Zinc in PDB 8aly: Cryo-Em Structure of Human Tankyrase 2 Sam-Parp Filament (G1032W Mutant)

Enzymatic activity of Cryo-Em Structure of Human Tankyrase 2 Sam-Parp Filament (G1032W Mutant)

All present enzymatic activity of Cryo-Em Structure of Human Tankyrase 2 Sam-Parp Filament (G1032W Mutant):
2.4.2.30;

Zinc Binding Sites:

Pages:

>>> Page 1 <<< Page 2, Binding sites: 11 - 20;

Binding sites:

The binding sites of Zinc atom in the Cryo-Em Structure of Human Tankyrase 2 Sam-Parp Filament (G1032W Mutant) (pdb code 8aly). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 20 binding sites of Zinc where determined in the Cryo-Em Structure of Human Tankyrase 2 Sam-Parp Filament (G1032W Mutant), PDB code: 8aly:
Jump to Zinc binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Zinc binding site 1 out of 20 in 8aly

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Zinc binding site 1 out of 20 in the Cryo-Em Structure of Human Tankyrase 2 Sam-Parp Filament (G1032W Mutant)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Cryo-Em Structure of Human Tankyrase 2 Sam-Parp Filament (G1032W Mutant) within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Zn1201

b:99.2
occ:1.00
SG E:CYS1089 2.3 54.5 1.0
ND1 E:HIS1084 2.3 60.7 1.0
CE1 E:HIS1084 3.1 60.7 1.0
SG E:CYS1081 3.2 50.5 1.0
CB E:CYS1089 3.2 54.5 1.0
CG E:HIS1084 3.3 60.7 1.0
CB E:HIS1084 3.7 60.7 1.0
N E:HIS1084 3.9 60.7 1.0
NE2 E:HIS1084 4.3 60.7 1.0
CA E:HIS1084 4.4 60.7 1.0
CD2 E:HIS1084 4.4 60.7 1.0
CB E:CYS1092 4.5 54.1 1.0
CA E:CYS1092 4.6 54.1 1.0
O E:HIS1084 4.6 60.7 1.0
O E:ILE1091 4.7 53.6 1.0
N E:CYS1092 4.7 54.1 1.0
CA E:CYS1089 4.7 54.5 1.0
C E:ILE1091 4.7 53.6 1.0
CB E:VAL1083 4.8 57.4 1.0
C E:HIS1084 4.9 60.7 1.0
CB E:CYS1081 4.9 50.5 1.0
N E:VAL1083 4.9 57.4 1.0

Zinc binding site 2 out of 20 in 8aly

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Zinc binding site 2 out of 20 in the Cryo-Em Structure of Human Tankyrase 2 Sam-Parp Filament (G1032W Mutant)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Cryo-Em Structure of Human Tankyrase 2 Sam-Parp Filament (G1032W Mutant) within 5.0Å range:
probe atom residue distance (Å) B Occ
J:Zn1201

b:123.4
occ:1.00
SG J:CYS1089 2.3 62.0 1.0
ND1 J:HIS1084 2.3 71.6 1.0
CG J:HIS1084 2.4 71.6 1.0
CB J:HIS1084 2.5 71.6 1.0
SG J:CYS1081 2.7 67.1 1.0
CE1 J:HIS1084 3.2 71.6 1.0
CD2 J:HIS1084 3.4 71.6 1.0
N J:HIS1084 3.5 71.6 1.0
CB J:CYS1089 3.5 62.0 1.0
CA J:HIS1084 3.6 71.6 1.0
CG2 J:VAL1083 3.6 69.5 1.0
NE2 J:HIS1084 3.8 71.6 1.0
CB J:CYS1081 4.1 67.1 1.0
O J:ILE1091 4.4 56.3 1.0
C J:HIS1084 4.5 71.6 1.0
C J:ILE1091 4.6 56.3 1.0
C J:VAL1083 4.6 69.5 1.0
O J:HIS1084 4.6 71.6 1.0
N J:CYS1092 4.8 55.5 1.0
CB J:ILE1091 4.8 56.3 1.0
CA J:CYS1089 4.9 62.0 1.0
CB J:VAL1083 4.9 69.5 1.0
CB J:CYS1092 4.9 55.5 1.0
CA J:CYS1092 5.0 55.5 1.0

Zinc binding site 3 out of 20 in 8aly

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Zinc binding site 3 out of 20 in the Cryo-Em Structure of Human Tankyrase 2 Sam-Parp Filament (G1032W Mutant)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Cryo-Em Structure of Human Tankyrase 2 Sam-Parp Filament (G1032W Mutant) within 5.0Å range:
probe atom residue distance (Å) B Occ
I:Zn1201

b:108.8
occ:1.00
SG I:CYS1089 2.3 58.3 1.0
ND1 I:HIS1084 2.3 74.0 1.0
CE1 I:HIS1084 3.1 74.0 1.0
SG I:CYS1081 3.2 65.5 1.0
CG I:HIS1084 3.4 74.0 1.0
CB I:CYS1089 3.5 58.3 1.0
CB I:HIS1084 3.8 74.0 1.0
O I:ILE1091 3.9 56.6 1.0
C I:ILE1091 4.1 56.6 1.0
N I:HIS1084 4.1 74.0 1.0
CA I:CYS1092 4.2 56.0 1.0
N I:CYS1092 4.2 56.0 1.0
CB I:CYS1092 4.2 56.0 1.0
NE2 I:HIS1084 4.3 74.0 1.0
CD2 I:HIS1084 4.4 74.0 1.0
O I:HIS1084 4.5 74.0 1.0
CA I:HIS1084 4.5 74.0 1.0
CB I:ILE1091 4.8 56.6 1.0
CA I:ILE1091 4.8 56.6 1.0
N I:ILE1091 4.9 56.6 1.0
CA I:CYS1089 4.9 58.3 1.0
CB I:CYS1081 4.9 65.5 1.0
C I:HIS1084 5.0 74.0 1.0

Zinc binding site 4 out of 20 in 8aly

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Zinc binding site 4 out of 20 in the Cryo-Em Structure of Human Tankyrase 2 Sam-Parp Filament (G1032W Mutant)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Cryo-Em Structure of Human Tankyrase 2 Sam-Parp Filament (G1032W Mutant) within 5.0Å range:
probe atom residue distance (Å) B Occ
H:Zn1201

b:99.0
occ:1.00
ND1 H:HIS1084 2.3 66.3 1.0
SG H:CYS1089 2.3 54.9 1.0
CE1 H:HIS1084 3.0 66.3 1.0
SG H:CYS1081 3.3 65.0 1.0
CB H:CYS1089 3.3 54.9 1.0
CG H:HIS1084 3.4 66.3 1.0
CB H:CYS1092 3.9 51.1 1.0
CB H:HIS1084 4.0 66.3 1.0
N H:HIS1084 4.0 66.3 1.0
CA H:CYS1092 4.1 51.1 1.0
NE2 H:HIS1084 4.2 66.3 1.0
N H:CYS1092 4.2 51.1 1.0
C H:ILE1091 4.3 53.4 1.0
O H:ILE1091 4.3 53.4 1.0
CD2 H:HIS1084 4.4 66.3 1.0
CA H:HIS1084 4.6 66.3 1.0
CB H:VAL1083 4.6 65.4 1.0
CA H:CYS1089 4.8 54.9 1.0
O H:HIS1084 4.8 66.3 1.0
N H:VAL1083 4.8 65.4 1.0

Zinc binding site 5 out of 20 in 8aly

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Zinc binding site 5 out of 20 in the Cryo-Em Structure of Human Tankyrase 2 Sam-Parp Filament (G1032W Mutant)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 5 of Cryo-Em Structure of Human Tankyrase 2 Sam-Parp Filament (G1032W Mutant) within 5.0Å range:
probe atom residue distance (Å) B Occ
G:Zn1201

b:90.8
occ:1.00
SG G:CYS1089 2.3 52.8 1.0
ND1 G:HIS1084 2.3 65.2 1.0
CG G:HIS1084 3.2 65.2 1.0
CE1 G:HIS1084 3.3 65.2 1.0
CB G:CYS1089 3.4 52.8 1.0
SG G:CYS1081 3.4 58.8 1.0
CB G:HIS1084 3.5 65.2 1.0
N G:HIS1084 3.6 65.2 1.0
CA G:HIS1084 4.1 65.2 1.0
CB G:CYS1092 4.2 49.9 1.0
CB G:VAL1083 4.2 62.8 1.0
CD2 G:HIS1084 4.3 65.2 1.0
NE2 G:HIS1084 4.4 65.2 1.0
CA G:CYS1092 4.5 49.9 1.0
N G:CYS1092 4.5 49.9 1.0
C G:ILE1091 4.5 50.4 1.0
O G:ILE1091 4.5 50.4 1.0
C G:VAL1083 4.6 62.8 1.0
N G:VAL1083 4.6 62.8 1.0
CA G:VAL1083 4.7 62.8 1.0
CA G:CYS1089 4.8 52.8 1.0
CG1 G:VAL1083 4.9 62.8 1.0

Zinc binding site 6 out of 20 in 8aly

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Zinc binding site 6 out of 20 in the Cryo-Em Structure of Human Tankyrase 2 Sam-Parp Filament (G1032W Mutant)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 6 of Cryo-Em Structure of Human Tankyrase 2 Sam-Parp Filament (G1032W Mutant) within 5.0Å range:
probe atom residue distance (Å) B Occ
F:Zn1201

b:87.0
occ:1.00
ND1 F:HIS1084 2.3 65.0 1.0
SG F:CYS1089 2.3 55.9 1.0
SG F:CYS1081 2.8 62.2 1.0
CE1 F:HIS1084 3.1 65.0 1.0
CB F:CYS1089 3.2 55.9 1.0
CG2 F:VAL1083 3.2 61.7 1.0
CG F:HIS1084 3.3 65.0 1.0
CB F:HIS1084 3.7 65.0 1.0
N F:HIS1084 3.8 65.0 1.0
CB F:CYS1092 4.0 52.6 1.0
NE2 F:HIS1084 4.3 65.0 1.0
CA F:CYS1092 4.3 52.6 1.0
CA F:HIS1084 4.3 65.0 1.0
CD2 F:HIS1084 4.4 65.0 1.0
O F:HIS1084 4.5 65.0 1.0
N F:CYS1092 4.5 52.6 1.0
CB F:CYS1081 4.5 62.2 1.0
CB F:VAL1083 4.6 61.7 1.0
O F:ILE1091 4.6 53.8 1.0
C F:ILE1091 4.6 53.8 1.0
CA F:CYS1089 4.6 55.9 1.0
N F:VAL1083 4.7 61.7 1.0
C F:VAL1083 4.8 61.7 1.0
C F:HIS1084 4.8 65.0 1.0
CA F:VAL1083 4.9 61.7 1.0

Zinc binding site 7 out of 20 in 8aly

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Zinc binding site 7 out of 20 in the Cryo-Em Structure of Human Tankyrase 2 Sam-Parp Filament (G1032W Mutant)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 7 of Cryo-Em Structure of Human Tankyrase 2 Sam-Parp Filament (G1032W Mutant) within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Zn1201

b:97.0
occ:1.00
SG D:CYS1089 2.3 58.7 1.0
ND1 D:HIS1084 2.3 70.8 1.0
CG D:HIS1084 2.3 70.8 1.0
SG D:CYS1081 2.9 59.5 1.0
CB D:HIS1084 2.9 70.8 1.0
CE1 D:HIS1084 2.9 70.8 1.0
CD2 D:HIS1084 2.9 70.8 1.0
NE2 D:HIS1084 3.2 70.8 1.0
CB D:CYS1089 3.5 58.7 1.0
N D:HIS1084 3.5 70.8 1.0
CG2 D:VAL1083 3.6 66.7 1.0
CA D:HIS1084 3.8 70.8 1.0
CB D:CYS1081 4.3 59.5 1.0
C D:VAL1083 4.7 66.7 1.0
C D:HIS1084 4.7 70.8 1.0
CA D:CYS1089 4.8 58.7 1.0
O D:ILE1091 4.8 53.9 1.0
O D:HIS1084 4.8 70.8 1.0
CB D:VAL1083 4.9 66.7 1.0
C D:ILE1091 4.9 53.9 1.0
N D:VAL1083 5.0 66.7 1.0
CB D:CYS1092 5.0 52.4 1.0

Zinc binding site 8 out of 20 in 8aly

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Zinc binding site 8 out of 20 in the Cryo-Em Structure of Human Tankyrase 2 Sam-Parp Filament (G1032W Mutant)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 8 of Cryo-Em Structure of Human Tankyrase 2 Sam-Parp Filament (G1032W Mutant) within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Zn1201

b:81.3
occ:1.00
SG C:CYS1089 2.3 60.2 1.0
ND1 C:HIS1084 2.3 67.1 1.0
SG C:CYS1081 2.5 60.5 1.0
CG C:HIS1084 3.0 67.1 1.0
CE1 C:HIS1084 3.2 67.1 1.0
CB C:CYS1089 3.3 60.2 1.0
CB C:HIS1084 3.4 67.1 1.0
N C:HIS1084 3.7 67.1 1.0
CD2 C:HIS1084 4.0 67.1 1.0
NE2 C:HIS1084 4.1 67.1 1.0
CA C:HIS1084 4.1 67.1 1.0
CB C:CYS1081 4.3 60.5 1.0
CB C:CYS1092 4.5 57.8 1.0
CA C:CYS1092 4.6 57.8 1.0
O C:ILE1091 4.6 55.6 1.0
CB C:VAL1083 4.7 66.2 1.0
CA C:CYS1089 4.7 60.2 1.0
N C:VAL1083 4.7 66.2 1.0
C C:ILE1091 4.7 55.6 1.0
N C:CYS1092 4.7 57.8 1.0
O C:HIS1084 4.8 67.1 1.0
C C:VAL1083 4.8 66.2 1.0
C C:HIS1084 4.8 67.1 1.0
CA C:VAL1083 5.0 66.2 1.0

Zinc binding site 9 out of 20 in 8aly

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Zinc binding site 9 out of 20 in the Cryo-Em Structure of Human Tankyrase 2 Sam-Parp Filament (G1032W Mutant)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 9 of Cryo-Em Structure of Human Tankyrase 2 Sam-Parp Filament (G1032W Mutant) within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn1201

b:105.6
occ:1.00
SG B:CYS1089 2.3 61.5 1.0
ND1 B:HIS1084 2.3 63.6 1.0
SG B:CYS1081 2.8 54.8 1.0
CG B:HIS1084 3.1 63.6 1.0
CE1 B:HIS1084 3.2 63.6 1.0
CB B:CYS1089 3.3 61.5 1.0
CB B:HIS1084 3.4 63.6 1.0
CG1 B:VAL1083 3.6 59.0 1.0
N B:HIS1084 3.7 63.6 1.0
CA B:HIS1084 4.1 63.6 1.0
CD2 B:HIS1084 4.2 63.6 1.0
NE2 B:HIS1084 4.2 63.6 1.0
CB B:CYS1081 4.6 54.8 1.0
CB B:CYS1092 4.6 62.3 1.0
CA B:CYS1092 4.7 62.3 1.0
C B:VAL1083 4.7 59.0 1.0
CA B:CYS1089 4.7 61.5 1.0
O B:ILE1091 4.8 54.1 1.0
N B:CYS1092 4.8 62.3 1.0
O B:HIS1084 4.8 63.6 1.0
C B:ILE1091 4.8 54.1 1.0
N B:VAL1083 4.8 59.0 1.0
C B:HIS1084 4.9 63.6 1.0
CB B:VAL1083 4.9 59.0 1.0

Zinc binding site 10 out of 20 in 8aly

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Zinc binding site 10 out of 20 in the Cryo-Em Structure of Human Tankyrase 2 Sam-Parp Filament (G1032W Mutant)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 10 of Cryo-Em Structure of Human Tankyrase 2 Sam-Parp Filament (G1032W Mutant) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn1201

b:101.2
occ:1.00
SG A:CYS1089 2.3 64.1 1.0
ND1 A:HIS1084 2.3 73.5 1.0
SG A:CYS1081 2.5 64.8 1.0
CB A:CYS1089 2.9 64.1 1.0
CG A:HIS1084 3.2 73.5 1.0
CE1 A:HIS1084 3.3 73.5 1.0
CB A:HIS1084 3.4 73.5 1.0
CG2 A:VAL1083 3.5 69.6 1.0
N A:HIS1084 3.7 73.5 1.0
CA A:HIS1084 4.1 73.5 1.0
CB A:CYS1092 4.1 62.7 1.0
CB A:CYS1081 4.3 64.8 1.0
CD2 A:HIS1084 4.4 73.5 1.0
NE2 A:HIS1084 4.4 73.5 1.0
CA A:CYS1089 4.4 64.1 1.0
CA A:CYS1092 4.6 62.7 1.0
N A:CYS1092 4.7 62.7 1.0
O A:HIS1084 4.7 73.5 1.0
C A:HIS1084 4.8 73.5 1.0
N A:VAL1083 4.8 69.6 1.0
C A:VAL1083 4.8 69.6 1.0
C A:ILE1091 4.8 60.2 1.0
O A:ASP1086 4.8 66.8 1.0
CB A:VAL1083 4.9 69.6 1.0
O A:ILE1091 4.9 60.2 1.0

Reference:

N.Pillay, L.Mariotti, M.Zaleska, O.Inian, M.Jessop, S.Hibbs, A.Desfosses, P.C.R.Hopkins, C.M.Templeton, F.Beuron, E.P.Morris, S.Guettler. Structural Basis of Tankyrase Activation By Polymerization. Nature V. 612 162 2022.
ISSN: ESSN 1476-4687
PubMed: 36418402
DOI: 10.1038/S41586-022-05449-8
Page generated: Sat Apr 8 07:44:27 2023

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