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Zinc in PDB 8fm1: Structure of Cbass CAP5 From Pseudomonas Syringae in the Absence of A Ligand (Apo Form Dimer)

Protein crystallography data

The structure of Structure of Cbass CAP5 From Pseudomonas Syringae in the Absence of A Ligand (Apo Form Dimer), PDB code: 8fm1 was solved by O.Rechkoblit, D.F.Kreitler, A.K.Aggarwal, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 112.73 / 3.16
Space group P 41 21 2
Cell size a, b, c (Å), α, β, γ (°) 159.428, 159.428, 433.875, 90, 90, 90
R / Rfree (%) 24 / 29.4

Zinc Binding Sites:

Pages:

>>> Page 1 <<< Page 2, Binding sites: 11 - 12;

Binding sites:

The binding sites of Zinc atom in the Structure of Cbass CAP5 From Pseudomonas Syringae in the Absence of A Ligand (Apo Form Dimer) (pdb code 8fm1). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 12 binding sites of Zinc where determined in the Structure of Cbass CAP5 From Pseudomonas Syringae in the Absence of A Ligand (Apo Form Dimer), PDB code: 8fm1:
Jump to Zinc binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Zinc binding site 1 out of 12 in 8fm1

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Zinc binding site 1 out of 12 in the Structure of Cbass CAP5 From Pseudomonas Syringae in the Absence of A Ligand (Apo Form Dimer)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structure of Cbass CAP5 From Pseudomonas Syringae in the Absence of A Ligand (Apo Form Dimer) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn401

b:110.0
occ:1.00
SG A:CYS87 2.3 116.2 1.0
SG A:CYS35 2.3 107.1 1.0
SG A:CYS90 2.3 129.8 1.0
SG A:CYS32 2.3 110.0 1.0
HG A:CYS87 2.6 139.5 1.0
HB2 A:CYS90 2.9 140.0 1.0
H A:CYS87 3.1 138.6 1.0
CB A:CYS90 3.2 116.7 1.0
HB3 A:CYS32 3.2 129.3 1.0
HG A:CYS35 3.2 128.5 1.0
CB A:CYS32 3.3 107.8 1.0
HG A:CYS32 3.4 132.0 1.0
H A:CYS90 3.4 143.3 1.0
HG A:CYS90 3.4 155.7 1.0
HB2 A:CYS32 3.5 129.3 1.0
HB3 A:CYS35 3.5 126.4 1.0
HB3 A:CYS87 3.6 140.5 1.0
CB A:CYS87 3.6 117.1 1.0
CB A:CYS35 3.6 105.3 1.0
HB3 A:CYS90 3.9 140.0 1.0
N A:CYS87 3.9 115.5 1.0
HB2 A:LEU34 3.9 126.0 1.0
N A:CYS90 4.0 119.5 1.0
H A:CYS35 4.1 126.7 1.0
CA A:CYS90 4.2 118.8 1.0
N A:CYS35 4.2 105.5 1.0
CA A:CYS87 4.3 117.4 1.0
HB2 A:CYS35 4.3 126.4 1.0
HB2 A:CYS87 4.4 140.5 1.0
H A:LEU34 4.4 122.1 1.0
CA A:CYS35 4.5 103.2 1.0
HB A:THR37 4.5 130.9 1.0
O A:CYS87 4.5 124.4 1.0
HA A:CYS90 4.6 142.5 1.0
OG1 A:THR37 4.6 109.5 1.0
H A:THR37 4.7 127.1 1.0
CA A:CYS32 4.7 104.0 1.0
C A:LEU34 4.7 106.6 1.0
HA A:LEU86 4.8 133.1 1.0
CB A:LEU34 4.8 105.0 1.0
C A:CYS87 4.8 118.5 1.0
HD23 A:LEU86 4.8 132.0 1.0
HB3 A:LEU86 4.9 133.9 1.0
HB3 A:LEU34 5.0 126.0 1.0

Zinc binding site 2 out of 12 in 8fm1

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Zinc binding site 2 out of 12 in the Structure of Cbass CAP5 From Pseudomonas Syringae in the Absence of A Ligand (Apo Form Dimer)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Structure of Cbass CAP5 From Pseudomonas Syringae in the Absence of A Ligand (Apo Form Dimer) within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn401

b:110.0
occ:1.00
SG B:CYS35 2.3 115.0 1.0
SG B:CYS90 2.3 105.9 1.0
SG B:CYS32 2.3 102.9 1.0
SG B:CYS87 2.3 111.5 1.0
HG B:CYS87 2.7 133.8 1.0
HB2 B:CYS90 2.9 131.5 1.0
H B:CYS87 3.1 124.3 1.0
HB3 B:CYS32 3.1 122.3 1.0
CB B:CYS32 3.2 101.9 1.0
CB B:CYS90 3.2 109.5 1.0
HG B:CYS35 3.3 138.0 1.0
HG B:CYS32 3.3 123.5 1.0
HB3 B:CYS35 3.3 129.8 1.0
HB2 B:CYS32 3.3 122.3 1.0
HG B:CYS90 3.4 127.1 1.0
H B:CYS35 3.5 123.3 1.0
CB B:CYS35 3.5 108.2 1.0
H B:CYS90 3.5 134.7 1.0
HB3 B:CYS87 3.6 133.0 1.0
CB B:CYS87 3.7 110.8 1.0
HB3 B:CYS90 3.9 131.5 1.0
N B:CYS35 3.9 102.7 1.0
N B:CYS87 3.9 103.6 1.0
HB2 B:LEU34 4.0 118.9 1.0
N B:CYS90 4.2 112.3 1.0
HB2 B:CYS35 4.2 129.8 1.0
CA B:CYS35 4.3 104.6 1.0
CA B:CYS90 4.3 112.5 1.0
HB B:THR37 4.3 124.4 1.0
CA B:CYS87 4.3 107.5 1.0
HB2 B:CYS87 4.4 133.0 1.0
H B:LEU34 4.4 116.0 1.0
H B:THR37 4.5 120.2 1.0
O B:CYS87 4.6 115.4 1.0
CA B:CYS32 4.6 95.9 1.0
HB3 B:LEU34 4.7 118.9 1.0
HA B:LEU86 4.7 119.1 1.0
HA B:CYS90 4.7 135.0 1.0
OG1 B:THR37 4.7 104.9 1.0
CB B:LEU34 4.7 99.1 1.0
C B:LEU34 4.7 102.9 1.0
HD23 B:LEU86 4.8 116.8 1.0
C B:CYS35 4.9 105.4 1.0
HB3 B:LEU86 4.9 118.8 1.0
C B:CYS87 4.9 110.7 1.0

Zinc binding site 3 out of 12 in 8fm1

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Zinc binding site 3 out of 12 in the Structure of Cbass CAP5 From Pseudomonas Syringae in the Absence of A Ligand (Apo Form Dimer)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Structure of Cbass CAP5 From Pseudomonas Syringae in the Absence of A Ligand (Apo Form Dimer) within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Zn401

b:110.0
occ:1.00
SG C:CYS87 2.3 127.5 1.0
SG C:CYS90 2.3 115.3 1.0
SG C:CYS32 2.3 111.5 1.0
SG C:CYS35 2.3 128.4 1.0
HG C:CYS87 2.8 153.0 1.0
HB2 C:CYS90 3.1 143.3 1.0
H C:CYS87 3.3 142.8 1.0
HG C:CYS35 3.3 154.1 1.0
HB3 C:CYS32 3.3 132.9 1.0
CB C:CYS32 3.3 110.8 1.0
HG C:CYS32 3.3 133.8 1.0
H C:CYS35 3.3 135.5 1.0
CB C:CYS90 3.4 119.4 1.0
HG C:CYS90 3.4 138.4 1.0
HB3 C:CYS35 3.4 135.5 1.0
CB C:CYS35 3.5 112.9 1.0
HB2 C:CYS32 3.5 132.9 1.0
CB C:CYS87 3.7 124.6 1.0
HB3 C:CYS87 3.7 149.5 1.0
H C:CYS90 3.7 147.6 1.0
HB2 C:LEU34 3.9 136.1 1.0
N C:CYS35 3.9 112.9 1.0
HB3 C:CYS90 4.0 143.3 1.0
N C:CYS87 4.0 119.0 1.0
CA C:CYS35 4.2 113.7 1.0
HB C:THR37 4.3 141.0 1.0
HB2 C:CYS35 4.3 135.5 1.0
N C:CYS90 4.3 123.0 1.0
CA C:CYS87 4.4 121.7 1.0
HB2 C:CYS87 4.4 149.5 1.0
H C:LEU34 4.5 129.3 1.0
CA C:CYS90 4.5 123.5 1.0
O C:CYS87 4.6 121.5 1.0
O C:CYS35 4.7 112.8 1.0
CB C:LEU34 4.7 113.4 1.0
CA C:CYS32 4.7 108.4 1.0
H C:THR37 4.8 143.1 1.0
C C:CYS35 4.8 113.9 1.0
C C:LEU34 4.8 113.4 1.0
HA C:LEU86 4.8 137.3 1.0
HB3 C:LEU34 4.9 136.1 1.0
HA C:CYS90 4.9 148.2 1.0
C C:CYS87 4.9 123.1 1.0
HD21 C:LEU86 4.9 134.7 1.0
HB3 C:LEU86 5.0 137.2 1.0

Zinc binding site 4 out of 12 in 8fm1

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Zinc binding site 4 out of 12 in the Structure of Cbass CAP5 From Pseudomonas Syringae in the Absence of A Ligand (Apo Form Dimer)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Structure of Cbass CAP5 From Pseudomonas Syringae in the Absence of A Ligand (Apo Form Dimer) within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Zn401

b:110.0
occ:1.00
SG D:CYS90 2.3 126.9 1.0
SG D:CYS87 2.3 132.7 1.0
SG D:CYS35 2.3 133.7 1.0
SG D:CYS32 2.3 140.7 1.0
HG D:CYS32 2.5 168.8 1.0
HG D:CYS87 2.8 159.2 1.0
HB2 D:CYS90 3.0 158.2 1.0
H D:CYS87 3.2 159.4 1.0
CB D:CYS90 3.2 131.9 1.0
HG D:CYS35 3.3 160.4 1.0
HB3 D:CYS32 3.3 153.5 1.0
CB D:CYS32 3.3 127.9 1.0
HB3 D:CYS35 3.4 150.8 1.0
HG D:CYS90 3.4 152.2 1.0
H D:CYS90 3.5 162.9 1.0
CB D:CYS35 3.5 125.7 1.0
HB2 D:CYS32 3.6 153.5 1.0
HB3 D:CYS87 3.6 158.6 1.0
CB D:CYS87 3.6 132.2 1.0
HB3 D:CYS90 3.9 158.2 1.0
N D:CYS87 4.0 132.8 1.0
HB2 D:LEU34 4.0 148.7 1.0
H D:CYS35 4.0 148.0 1.0
N D:CYS90 4.1 135.8 1.0
N D:CYS35 4.1 123.3 1.0
HB2 D:CYS35 4.2 150.8 1.0
CA D:CYS90 4.3 135.4 1.0
CA D:CYS87 4.3 134.5 1.0
HB2 D:CYS87 4.3 158.6 1.0
H D:LEU34 4.4 145.9 1.0
CA D:CYS35 4.4 123.6 1.0
HB D:THR37 4.4 158.0 1.0
O D:CYS87 4.6 135.5 1.0
C D:LEU34 4.6 123.5 1.0
HA D:CYS90 4.7 162.5 1.0
H D:THR37 4.7 149.3 1.0
CA D:CYS32 4.7 124.2 1.0
CB D:LEU34 4.8 124.0 1.0
HA D:LEU86 4.8 153.5 1.0
C D:CYS87 4.8 136.1 1.0
OG1 D:THR37 4.8 131.0 1.0
HD23 D:LEU86 4.8 149.1 1.0
HB3 D:LEU86 4.9 153.0 1.0
HB3 D:LEU34 4.9 148.7 1.0
N D:LEU34 5.0 121.6 1.0
C D:CYS32 5.0 122.2 1.0

Zinc binding site 5 out of 12 in 8fm1

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Zinc binding site 5 out of 12 in the Structure of Cbass CAP5 From Pseudomonas Syringae in the Absence of A Ligand (Apo Form Dimer)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 5 of Structure of Cbass CAP5 From Pseudomonas Syringae in the Absence of A Ligand (Apo Form Dimer) within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Zn401

b:110.0
occ:1.00
SG E:CYS35 2.3 130.3 1.0
SG E:CYS32 2.3 138.6 1.0
SG E:CYS87 2.3 134.7 1.0
SG E:CYS90 2.3 142.3 1.0
HG E:CYS87 2.8 161.7 1.0
HB2 E:CYS90 2.9 170.2 1.0
HB3 E:CYS35 3.2 153.3 1.0
HB3 E:CYS32 3.2 158.8 1.0
CB E:CYS32 3.2 132.4 1.0
H E:CYS87 3.2 164.0 1.0
CB E:CYS90 3.2 141.8 1.0
HG E:CYS32 3.3 166.4 1.0
HB2 E:CYS32 3.3 158.8 1.0
HG E:CYS35 3.3 156.4 1.0
CB E:CYS35 3.4 127.8 1.0
HG E:CYS90 3.4 170.8 1.0
H E:CYS35 3.4 155.5 1.0
H E:CYS90 3.5 173.5 1.0
CB E:CYS87 3.7 137.1 1.0
HB3 E:CYS87 3.8 164.6 1.0
HB3 E:CYS90 3.9 170.2 1.0
N E:CYS35 4.0 129.6 1.0
N E:CYS87 4.0 136.7 1.0
N E:CYS90 4.1 144.6 1.0
HB2 E:CYS35 4.1 153.3 1.0
HB3 E:LEU34 4.2 156.4 1.0
CA E:CYS35 4.2 131.3 1.0
CA E:CYS90 4.3 143.2 1.0
HG23 E:THR37 4.4 160.1 1.0
CA E:CYS87 4.4 139.6 1.0
O E:CYS87 4.4 143.1 1.0
HB2 E:CYS87 4.5 164.6 1.0
H E:LEU34 4.5 149.2 1.0
CA E:CYS32 4.6 129.2 1.0
H E:THR37 4.7 157.3 1.0
HA E:CYS90 4.7 171.8 1.0
HA E:LEU86 4.7 160.5 1.0
H E:GLY36 4.8 154.9 1.0
C E:CYS87 4.8 142.7 1.0
C E:CYS35 4.8 129.9 1.0
HG22 E:THR37 4.9 160.1 1.0
C E:LEU34 4.9 127.8 1.0
HA E:CYS32 5.0 155.0 1.0

Zinc binding site 6 out of 12 in 8fm1

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Zinc binding site 6 out of 12 in the Structure of Cbass CAP5 From Pseudomonas Syringae in the Absence of A Ligand (Apo Form Dimer)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 6 of Structure of Cbass CAP5 From Pseudomonas Syringae in the Absence of A Ligand (Apo Form Dimer) within 5.0Å range:
probe atom residue distance (Å) B Occ
F:Zn401

b:110.0
occ:1.00
SG F:CYS32 2.3 114.2 1.0
SG F:CYS87 2.3 125.3 1.0
SG F:CYS35 2.3 126.3 1.0
SG F:CYS90 2.3 122.4 1.0
HG F:CYS87 2.8 150.4 1.0
HG F:CYS35 2.9 151.6 1.0
HB3 F:CYS35 3.0 142.3 1.0
H F:CYS35 3.0 135.5 1.0
HB3 F:CYS32 3.0 135.6 1.0
HB2 F:CYS90 3.1 145.1 1.0
CB F:CYS32 3.1 113.0 1.0
CB F:CYS35 3.2 118.5 1.0
H F:CYS87 3.3 140.0 1.0
HB2 F:CYS32 3.3 135.6 1.0
HG F:CYS90 3.3 146.9 1.0
CB F:CYS90 3.4 120.9 1.0
HG F:CYS32 3.4 137.0 1.0
H F:CYS90 3.6 149.4 1.0
HB3 F:CYS87 3.6 145.1 1.0
CB F:CYS87 3.7 120.9 1.0
N F:CYS35 3.7 112.9 1.0
HG22 F:THR37 3.9 141.8 1.0
HB2 F:CYS35 4.0 142.3 1.0
HB3 F:CYS90 4.0 145.1 1.0
CA F:CYS35 4.0 115.0 1.0
N F:CYS87 4.1 116.7 1.0
HB2 F:LEU34 4.1 136.3 1.0
N F:CYS90 4.2 124.5 1.0
H F:LEU34 4.3 134.0 1.0
HB2 F:CYS87 4.4 145.1 1.0
CA F:CYS87 4.4 119.3 1.0
CA F:CYS90 4.4 125.1 1.0
CA F:CYS32 4.6 111.0 1.0
H F:THR37 4.6 137.6 1.0
HG21 F:THR37 4.7 141.8 1.0
C F:CYS35 4.7 114.9 1.0
CG2 F:THR37 4.7 118.2 1.0
O F:CYS87 4.7 121.2 1.0
HA F:CYS35 4.8 137.9 1.0
C F:LEU34 4.8 114.4 1.0
HA F:CYS90 4.8 150.1 1.0
HA F:LEU86 4.9 136.6 1.0
H F:GLY36 4.9 135.7 1.0
C F:CYS87 4.9 121.0 1.0
C F:CYS32 4.9 109.2 1.0
HA F:CYS32 4.9 133.2 1.0
N F:LEU34 5.0 111.7 1.0
CB F:LEU34 5.0 113.6 1.0

Zinc binding site 7 out of 12 in 8fm1

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Zinc binding site 7 out of 12 in the Structure of Cbass CAP5 From Pseudomonas Syringae in the Absence of A Ligand (Apo Form Dimer)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 7 of Structure of Cbass CAP5 From Pseudomonas Syringae in the Absence of A Ligand (Apo Form Dimer) within 5.0Å range:
probe atom residue distance (Å) B Occ
G:Zn401

b:110.0
occ:1.00
SG G:CYS87 2.3 147.4 1.0
SG G:CYS32 2.3 138.3 1.0
SG G:CYS35 2.3 134.3 1.0
SG G:CYS90 2.3 148.8 1.0
HG G:CYS32 2.6 166.0 1.0
HG G:CYS87 2.8 176.9 1.0
HB3 G:CYS35 2.9 162.1 1.0
HB2 G:CYS90 3.0 169.8 1.0
CB G:CYS35 3.2 135.0 1.0
HB3 G:CYS32 3.2 162.8 1.0
H G:CYS87 3.2 169.4 1.0
H G:CYS35 3.3 158.5 1.0
CB G:CYS90 3.3 141.5 1.0
CB G:CYS32 3.3 135.7 1.0
HG G:CYS90 3.4 178.6 1.0
HG G:CYS35 3.4 161.1 1.0
H G:CYS90 3.5 172.2 1.0
HB2 G:CYS32 3.5 162.8 1.0
HB3 G:CYS87 3.6 172.8 1.0
CB G:CYS87 3.6 144.0 1.0
N G:CYS35 3.8 132.1 1.0
HB2 G:CYS35 3.9 162.1 1.0
HB3 G:CYS90 3.9 169.8 1.0
HB2 G:LEU34 4.0 156.8 1.0
N G:CYS87 4.0 141.1 1.0
CA G:CYS35 4.1 135.2 1.0
N G:CYS90 4.1 143.5 1.0
CA G:CYS90 4.3 144.7 1.0
HB2 G:CYS87 4.4 172.8 1.0
CA G:CYS87 4.4 145.5 1.0
H G:LEU34 4.4 153.1 1.0
H G:GLY36 4.5 158.9 1.0
H G:THR37 4.6 165.5 1.0
O G:CYS87 4.6 144.8 1.0
CA G:CYS32 4.7 132.4 1.0
HB G:THR37 4.7 168.1 1.0
HA G:CYS90 4.7 173.6 1.0
C G:LEU34 4.7 129.7 1.0
HA G:CYS35 4.8 162.3 1.0
C G:CYS35 4.8 134.4 1.0
HA G:LEU86 4.8 166.2 1.0
CB G:LEU34 4.9 130.6 1.0
C G:CYS87 4.9 145.8 1.0
N G:GLY36 4.9 132.4 1.0
C G:CYS32 5.0 129.8 1.0

Zinc binding site 8 out of 12 in 8fm1

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Zinc binding site 8 out of 12 in the Structure of Cbass CAP5 From Pseudomonas Syringae in the Absence of A Ligand (Apo Form Dimer)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 8 of Structure of Cbass CAP5 From Pseudomonas Syringae in the Absence of A Ligand (Apo Form Dimer) within 5.0Å range:
probe atom residue distance (Å) B Occ
H:Zn401

b:110.0
occ:1.00
SG H:CYS87 2.3 137.9 1.0
SG H:CYS35 2.3 126.5 1.0
SG H:CYS32 2.3 133.9 1.0
SG H:CYS90 2.3 125.4 1.0
HG H:CYS87 2.7 165.4 1.0
HB2 H:CYS90 2.8 159.4 1.0
HB3 H:CYS35 3.1 149.1 1.0
CB H:CYS90 3.2 132.8 1.0
H H:CYS87 3.2 151.8 1.0
H H:CYS35 3.2 143.8 1.0
CB H:CYS35 3.3 124.2 1.0
HB3 H:CYS32 3.3 143.5 1.0
HG H:CYS32 3.3 160.6 1.0
CB H:CYS32 3.3 119.6 1.0
HG H:CYS35 3.4 151.8 1.0
H H:CYS90 3.4 160.8 1.0
HG H:CYS90 3.4 150.5 1.0
HB2 H:CYS32 3.5 143.5 1.0
HB3 H:CYS87 3.6 152.7 1.0
CB H:CYS87 3.6 127.3 1.0
N H:CYS35 3.7 119.9 1.0
HB3 H:CYS90 3.8 159.4 1.0
N H:CYS87 4.0 126.5 1.0
HB2 H:LEU34 4.0 145.9 1.0
N H:CYS90 4.0 134.0 1.0
HB2 H:CYS35 4.1 149.1 1.0
CA H:CYS35 4.1 120.3 1.0
HB3 H:LEU34 4.1 145.9 1.0
CA H:CYS90 4.2 136.5 1.0
H H:LEU34 4.3 140.0 1.0
CA H:CYS87 4.3 127.8 1.0
HB2 H:CYS87 4.4 152.7 1.0
CB H:LEU34 4.4 121.6 1.0
O H:CYS87 4.5 130.2 1.0
C H:LEU34 4.5 119.7 1.0
HA H:CYS90 4.7 163.8 1.0
CA H:CYS32 4.7 115.8 1.0
H H:THR37 4.8 140.7 1.0
C H:CYS35 4.8 118.1 1.0
C H:CYS87 4.8 130.1 1.0
HA H:LEU86 4.8 146.4 1.0
HB H:THR37 4.8 150.8 1.0
CA H:LEU34 4.9 119.7 1.0
N H:LEU34 4.9 116.6 1.0
HA H:CYS35 4.9 144.3 1.0
HB3 H:LEU86 4.9 146.9 1.0

Zinc binding site 9 out of 12 in 8fm1

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Zinc binding site 9 out of 12 in the Structure of Cbass CAP5 From Pseudomonas Syringae in the Absence of A Ligand (Apo Form Dimer)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 9 of Structure of Cbass CAP5 From Pseudomonas Syringae in the Absence of A Ligand (Apo Form Dimer) within 5.0Å range:
probe atom residue distance (Å) B Occ
I:Zn401

b:110.0
occ:1.00
SG I:CYS32 2.3 143.6 1.0
SG I:CYS35 2.3 159.7 1.0
SG I:CYS90 2.3 148.4 1.0
SG I:CYS87 2.3 164.4 1.0
HG I:CYS87 2.7 197.3 1.0
HB2 I:CYS90 2.7 186.9 1.0
HB3 I:CYS32 2.9 167.8 1.0
HB3 I:CYS35 3.1 175.4 1.0
CB I:CYS32 3.1 139.8 1.0
CB I:CYS90 3.1 155.8 1.0
HB2 I:CYS32 3.3 167.8 1.0
H I:CYS87 3.3 184.2 1.0
CB I:CYS35 3.3 146.2 1.0
HG I:CYS35 3.3 191.7 1.0
HG I:CYS32 3.4 172.3 1.0
HG I:CYS90 3.4 178.1 1.0
H I:CYS90 3.6 185.0 1.0
H I:CYS35 3.7 168.5 1.0
HB3 I:CYS90 3.7 186.9 1.0
CB I:CYS87 3.8 155.2 1.0
HB3 I:CYS87 3.9 186.3 1.0
HG21 I:THR37 3.9 172.8 1.0
N I:CYS35 3.9 140.4 1.0
HB2 I:CYS35 4.0 175.4 1.0
N I:CYS87 4.1 153.5 1.0
HB2 I:LEU34 4.1 169.1 1.0
N I:CYS90 4.2 154.2 1.0
CA I:CYS35 4.2 141.7 1.0
CA I:CYS90 4.3 154.8 1.0
H I:LEU34 4.4 159.5 1.0
HG22 I:THR37 4.4 172.8 1.0
CA I:CYS87 4.5 155.9 1.0
O I:CYS87 4.5 152.4 1.0
CA I:CYS32 4.5 137.8 1.0
HB2 I:CYS87 4.5 186.3 1.0
C I:LEU34 4.7 142.0 1.0
CG2 I:THR37 4.7 144.0 1.0
HB3 I:LEU86 4.7 180.5 1.0
HA I:CYS90 4.7 185.8 1.0
H I:THR37 4.9 169.0 1.0
C I:CYS87 4.9 155.4 1.0
C I:CYS32 4.9 138.6 1.0
HA I:LEU86 4.9 179.9 1.0
C I:CYS35 4.9 138.6 1.0
O I:CYS32 4.9 139.3 1.0
HA I:CYS32 4.9 165.4 1.0
CB I:LEU34 5.0 140.9 1.0
HD22 I:LEU86 5.0 172.9 1.0

Zinc binding site 10 out of 12 in 8fm1

Go back to Zinc Binding Sites List in 8fm1
Zinc binding site 10 out of 12 in the Structure of Cbass CAP5 From Pseudomonas Syringae in the Absence of A Ligand (Apo Form Dimer)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 10 of Structure of Cbass CAP5 From Pseudomonas Syringae in the Absence of A Ligand (Apo Form Dimer) within 5.0Å range:
probe atom residue distance (Å) B Occ
J:Zn401

b:110.0
occ:1.00
SG J:CYS32 2.3 146.1 1.0
SG J:CYS35 2.3 148.7 1.0
SG J:CYS87 2.3 154.0 1.0
SG J:CYS90 2.3 161.7 1.0
HG J:CYS32 2.7 175.3 1.0
HG J:CYS87 3.0 184.8 1.0
HB3 J:CYS35 3.2 170.3 1.0
HG J:CYS90 3.2 194.0 1.0
H J:CYS35 3.2 168.9 1.0
HG J:CYS35 3.3 178.5 1.0
CB J:CYS35 3.4 141.9 1.0
HB2 J:CYS90 3.4 189.2 1.0
CB J:CYS32 3.5 142.8 1.0
CB J:CYS90 3.6 157.7 1.0
HB3 J:CYS32 3.6 171.4 1.0
HB2 J:CYS32 3.6 171.4 1.0
H J:CYS90 3.7 189.2 1.0
HB2 J:LEU34 3.7 167.8 1.0
N J:CYS35 3.8 140.7 1.0
CB J:CYS87 3.8 152.7 1.0
HB3 J:CYS87 3.8 183.2 1.0
H J:CYS87 4.0 184.2 1.0
HG21 J:THR37 4.0 171.5 1.0
CA J:CYS35 4.1 142.7 1.0
HB2 J:CYS35 4.2 170.3 1.0
HB3 J:CYS90 4.2 189.2 1.0
N J:CYS90 4.3 157.7 1.0
H J:LEU34 4.4 162.7 1.0
N J:CYS87 4.4 153.5 1.0
HB2 J:CYS87 4.5 183.2 1.0
CA J:CYS90 4.5 159.7 1.0
CB J:LEU34 4.6 139.8 1.0
CA J:CYS87 4.6 155.0 1.0
C J:LEU34 4.7 138.4 1.0
HB3 J:LEU34 4.7 167.8 1.0
C J:CYS35 4.8 140.5 1.0
HG22 J:THR37 4.8 171.5 1.0
O J:CYS87 4.8 156.0 1.0
CG2 J:THR37 4.8 142.9 1.0
CA J:CYS32 4.9 140.7 1.0
HA J:CYS90 4.9 191.6 1.0
H J:THR37 4.9 172.1 1.0
HA J:CYS35 5.0 171.2 1.0
N J:LEU34 5.0 135.6 1.0
HD12 J:LEU34 5.0 172.8 1.0
CA J:LEU34 5.0 136.7 1.0

Reference:

O.Rechkoblit, D.Sciaky, D.F.Kreitler, A.Buku, J.Kottur, A.K.Aggarwal. Activation of Cbass-CAP5 Endonuclease Immune Effector By Cyclic Nucleotides: A View at High Resolution Nat.Struct.Mol.Biol. 2024.
ISSN: ESSN 1545-9985
DOI: 10.1038/S41594-024-01220-X
Page generated: Wed Oct 30 20:27:22 2024

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