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Zinc in PDB 7v9o: Crystal Structure of the Lanthipeptide Zinc-Metallopeptidase Eryp Mutant E802R From Saccharopolyspora Erythraea

Enzymatic activity of Crystal Structure of the Lanthipeptide Zinc-Metallopeptidase Eryp Mutant E802R From Saccharopolyspora Erythraea

All present enzymatic activity of Crystal Structure of the Lanthipeptide Zinc-Metallopeptidase Eryp Mutant E802R From Saccharopolyspora Erythraea:
3.4.11.2;

Protein crystallography data

The structure of Crystal Structure of the Lanthipeptide Zinc-Metallopeptidase Eryp Mutant E802R From Saccharopolyspora Erythraea, PDB code: 7v9o was solved by C.Zhao, N.L.Zhao, R.Bao, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 19.57 / 1.77
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 58.909, 143.583, 60.58, 90, 114.76, 90
R / Rfree (%) 13.9 / 17.1

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of the Lanthipeptide Zinc-Metallopeptidase Eryp Mutant E802R From Saccharopolyspora Erythraea (pdb code 7v9o). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the Crystal Structure of the Lanthipeptide Zinc-Metallopeptidase Eryp Mutant E802R From Saccharopolyspora Erythraea, PDB code: 7v9o:

Zinc binding site 1 out of 1 in 7v9o

Go back to Zinc Binding Sites List in 7v9o
Zinc binding site 1 out of 1 in the Crystal Structure of the Lanthipeptide Zinc-Metallopeptidase Eryp Mutant E802R From Saccharopolyspora Erythraea


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 the Lanthipeptide Zinc-Metallopeptidase Eryp Mutant E802R From Saccharopolyspora Erythraea within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn901

b:15.4
occ:0.44
 OE2 A:GLU329 1.9 15.1 1.0
O A:HOH1847 2.0 21.6 1.0
NE2 A:HIS306 2.1 12.0 1.0
NE2 A:HIS310 2.1 12.7 1.0
CD2 A:HIS306 2.8 11.7 1.0
CD A:GLU329 2.9 13.7 1.0
CE1 A:HIS310 3.0 13.6 1.0
CD2 A:HIS310 3.1 11.9 1.0
OE1 A:GLU329 3.1 15.9 1.0
CE1 A:HIS306 3.2 14.8 1.0
O A:HOH1382 3.6 16.6 1.0
CE2 A:TYR392 3.9 13.6 1.0
CG A:HIS306 4.1 11.4 1.0
OE1 A:GLU275 4.1 12.5 1.0
OH A:TYR392 4.1 16.5 1.0
ND1 A:HIS310 4.2 11.5 1.0
ND1 A:HIS306 4.2 12.8 1.0
CG A:HIS310 4.2 9.6 1.0
CG A:GLU329 4.2 9.2 1.0
CZ A:TYR392 4.4 14.6 1.0
OE2 A:GLU307 4.4 15.2 1.0
CB A:ALA332 4.6 12.6 1.0
CA A:GLU329 4.6 9.3 1.0
CB A:GLU329 4.7 10.6 1.0
CD A:GLU275 4.7 11.3 1.0
OE1 A:GLU307 4.7 20.3 1.0
OE2 A:GLU275 4.8 11.0 1.0
O A:HOH1707 4.9 28.3 1.0
CD2 A:TYR392 4.9 12.4 1.0
CD A:GLU307 4.9 15.6 1.0

Reference:

C.Zhao, W.Sheng, Y.Wang, J.Zheng, X.Xie, Y.Liang, W.Wei, R.Bao, H.Wang. Conformational Remodeling Enhances Activity of Lanthipeptide Zinc-Metallopeptidases. Nat.Chem.Biol. V. 18 724 2022.
ISSN: ESSN 1552-4469
PubMed: 35513512
DOI: 10.1038/S41589-022-01018-2
Page generated: Wed Oct 30 12:37:17 2024

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