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Zinc in PDB 3p1v: Crystal Structure of A Metallo-Endopeptidases (BACOVA_00663) From Bacteroides Ovatus at 1.93 A Resolution

Protein crystallography data

The structure of Crystal Structure of A Metallo-Endopeptidases (BACOVA_00663) From Bacteroides Ovatus at 1.93 A Resolution, PDB code: 3p1v was solved by Joint Center For Structural Genomics (Jcsg), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 48.91 / 1.93
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 72.919, 84.963, 139.758, 90.00, 99.56, 90.00
R / Rfree (%) 17 / 20.7

Other elements in 3p1v:

The structure of Crystal Structure of A Metallo-Endopeptidases (BACOVA_00663) From Bacteroides Ovatus at 1.93 A Resolution also contains other interesting chemical elements:

Potassium (K) 2 atoms
Chlorine (Cl) 3 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of A Metallo-Endopeptidases (BACOVA_00663) From Bacteroides Ovatus at 1.93 A Resolution (pdb code 3p1v). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the Crystal Structure of A Metallo-Endopeptidases (BACOVA_00663) From Bacteroides Ovatus at 1.93 A Resolution, PDB code: 3p1v:
Jump to Zinc binding site number: 1; 2; 3; 4;

Zinc binding site 1 out of 4 in 3p1v

Go back to Zinc Binding Sites List in 3p1v
Zinc binding site 1 out of 4 in the Crystal Structure of A Metallo-Endopeptidases (BACOVA_00663) From Bacteroides Ovatus at 1.93 A Resolution


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of A Metallo-Endopeptidases (BACOVA_00663) From Bacteroides Ovatus at 1.93 A Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn426

b:25.9
occ:0.60
O2 A:PO4433 1.9 55.5 1.0
OD1 A:ASP322 2.0 21.1 1.0
NE2 A:HIS315 2.1 20.4 1.0
NE2 A:HIS311 2.2 22.2 1.0
P A:PO4433 2.5 52.5 1.0
O1 A:PO4433 2.7 56.1 1.0
O3 A:PO4433 2.8 61.0 1.0
CG A:ASP322 2.8 22.1 1.0
OD2 A:ASP322 2.9 24.2 1.0
CE1 A:HIS315 3.1 20.5 1.0
CD2 A:HIS311 3.1 22.4 1.0
CD2 A:HIS315 3.1 20.6 1.0
CE1 A:HIS311 3.2 22.1 1.0
O4 A:PO4433 4.0 60.4 1.0
OE1 A:GLU312 4.1 30.4 1.0
CB A:ASP322 4.2 21.5 1.0
ND1 A:HIS315 4.2 21.7 1.0
CG A:HIS315 4.2 20.5 1.0
CG A:HIS311 4.2 21.5 1.0
ND1 A:HIS311 4.3 23.3 1.0
OH A:TYR324 4.4 27.5 1.0
CE2 A:TYR324 4.4 22.9 1.0
CE A:MSE400 4.5 15.5 1.0
O A:HOH854 4.7 42.6 1.0
CA A:ASP322 4.8 20.6 1.0
CZ A:TYR324 4.9 26.6 1.0
CD A:GLU312 4.9 31.0 1.0

Zinc binding site 2 out of 4 in 3p1v

Go back to Zinc Binding Sites List in 3p1v
Zinc binding site 2 out of 4 in the Crystal Structure of A Metallo-Endopeptidases (BACOVA_00663) From Bacteroides Ovatus at 1.93 A Resolution


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Crystal Structure of A Metallo-Endopeptidases (BACOVA_00663) From Bacteroides Ovatus at 1.93 A Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn427

b:21.8
occ:1.00
OE2 A:GLU323 2.0 21.1 1.0
SG A:CYS412 2.3 20.1 1.0
SG A:CYS409 2.4 22.6 1.0
SG A:CYS398 2.4 21.1 1.0
CD A:GLU323 2.9 19.5 1.0
OE1 A:GLU323 3.2 24.4 1.0
CB A:CYS412 3.2 17.4 1.0
CB A:CYS398 3.4 17.6 1.0
CB A:CYS409 3.4 19.4 1.0
N A:CYS409 3.8 20.5 1.0
CA A:CYS409 4.2 20.7 1.0
N A:CYS412 4.2 21.6 1.0
ND2 A:ASN345 4.2 18.6 1.0
CA A:CYS412 4.2 19.8 1.0
CG A:GLU323 4.3 20.0 1.0
CB A:MSE400 4.3 15.4 1.0
CB A:ASN345 4.4 19.6 1.0
CG A:MSE400 4.4 17.6 1.0
CD A:PRO394 4.6 23.1 1.0
O A:CYS409 4.8 23.3 1.0
C A:CYS409 4.8 25.1 1.0
CA A:CYS398 4.8 19.2 1.0
CG A:ASN345 4.8 31.3 1.0
CG A:PRO394 4.8 27.6 1.0
C A:PHE408 5.0 24.6 1.0
N A:MSE400 5.0 17.3 1.0

Zinc binding site 3 out of 4 in 3p1v

Go back to Zinc Binding Sites List in 3p1v
Zinc binding site 3 out of 4 in the Crystal Structure of A Metallo-Endopeptidases (BACOVA_00663) From Bacteroides Ovatus at 1.93 A Resolution


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Crystal Structure of A Metallo-Endopeptidases (BACOVA_00663) From Bacteroides Ovatus at 1.93 A Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn426

b:68.7
occ:0.50
OD1 B:ASP322 2.2 67.0 1.0
NE2 B:HIS315 2.2 54.4 1.0
O B:HOH546 2.2 55.8 1.0
NE2 B:HIS311 2.2 57.1 1.0
CG B:ASP322 2.9 66.7 1.0
OD2 B:ASP322 3.0 74.3 1.0
CD2 B:HIS311 3.1 56.8 1.0
CD2 B:HIS315 3.1 53.1 1.0
CE1 B:HIS315 3.2 53.7 1.0
CE1 B:HIS311 3.3 58.3 1.0
OE1 B:GLU312 3.8 60.7 1.0
CG B:HIS311 4.3 56.7 1.0
CG B:HIS315 4.3 49.8 1.0
OH B:TYR324 4.3 77.1 1.0
ND1 B:HIS315 4.3 52.5 1.0
ND1 B:HIS311 4.4 59.6 1.0
CB B:ASP322 4.4 61.0 1.0
CE2 B:TYR324 4.5 76.6 1.0
CE B:MSE400 4.6 53.3 1.0
CD B:GLU312 4.7 69.5 1.0
CZ B:TYR324 4.9 82.3 1.0
OE2 B:GLU312 4.9 72.2 1.0
CA B:ASP322 5.0 59.0 1.0

Zinc binding site 4 out of 4 in 3p1v

Go back to Zinc Binding Sites List in 3p1v
Zinc binding site 4 out of 4 in the Crystal Structure of A Metallo-Endopeptidases (BACOVA_00663) From Bacteroides Ovatus at 1.93 A Resolution


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Crystal Structure of A Metallo-Endopeptidases (BACOVA_00663) From Bacteroides Ovatus at 1.93 A Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn427

b:60.3
occ:1.00
OE2 B:GLU323 2.2 54.6 1.0
SG B:CYS412 2.3 58.8 1.0
SG B:CYS409 2.4 63.0 1.0
SG B:CYS398 2.5 63.5 1.0
CD B:GLU323 3.1 73.3 1.0
CB B:CYS412 3.2 55.5 1.0
CB B:CYS398 3.2 62.5 1.0
OE1 B:GLU323 3.2 67.8 1.0
CB B:CYS409 3.4 61.6 1.0
N B:CYS409 3.8 60.4 1.0
CA B:CYS409 4.1 61.3 1.0
N B:CYS412 4.2 56.3 1.0
ND2 B:ASN345 4.2 49.6 1.0
CA B:CYS412 4.2 54.8 1.0
CB B:MSE400 4.3 53.4 1.0
CB B:ASN345 4.4 53.2 1.0
CG B:MSE400 4.4 55.7 1.0
CG B:GLU323 4.5 70.7 1.0
CA B:CYS398 4.7 64.8 1.0
O B:CYS409 4.7 62.5 1.0
C B:CYS409 4.8 64.7 1.0
CD B:PRO394 4.8 64.8 1.0
CG B:ASN345 4.9 60.9 1.0
C B:PHE408 4.9 63.4 1.0
N B:MSE400 4.9 57.4 1.0
CG B:PRO394 5.0 67.9 1.0

Reference:

Joint Center For Structural Genomics (Jcsg), Joint Center For Structural Genomics (Jcsg). N/A N/A.
Page generated: Sat Oct 26 11:15:36 2024

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