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Zinc in PDB 7v9n: Crystal Structure of the Lanthipeptide Zinc-Metallopeptidase Eryp From Saccharopolyspora Erythraea in Closed State

Enzymatic activity of Crystal Structure of the Lanthipeptide Zinc-Metallopeptidase Eryp From Saccharopolyspora Erythraea in Closed State

All present enzymatic activity of Crystal Structure of the Lanthipeptide Zinc-Metallopeptidase Eryp From Saccharopolyspora Erythraea in Closed State:
3.4.11.2;

Protein crystallography data

The structure of Crystal Structure of the Lanthipeptide Zinc-Metallopeptidase Eryp From Saccharopolyspora Erythraea in Closed State, PDB code: 7v9n 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) 32.08 / 1.90
Space group P 43 21 2
Cell size a, b, c (Å), α, β, γ (°) 153.577, 153.577, 98.419, 90, 90, 90
R / Rfree (%) 15.4 / 18.1

Other elements in 7v9n:

The structure of Crystal Structure of the Lanthipeptide Zinc-Metallopeptidase Eryp From Saccharopolyspora Erythraea in Closed State also contains other interesting chemical elements:

Calcium (Ca) 1 atom

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of the Lanthipeptide Zinc-Metallopeptidase Eryp From Saccharopolyspora Erythraea in Closed State (pdb code 7v9n). 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 From Saccharopolyspora Erythraea in Closed State, PDB code: 7v9n:

Zinc binding site 1 out of 1 in 7v9n

Go back to Zinc Binding Sites List in 7v9n
Zinc binding site 1 out of 1 in the Crystal Structure of the Lanthipeptide Zinc-Metallopeptidase Eryp From Saccharopolyspora Erythraea in Closed State


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 From Saccharopolyspora Erythraea in Closed State within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn901

b:19.4
occ:1.00
 NE2 A:HIS306 2.0 17.3 1.0
O A:HOH1038 2.0 21.0 1.0
NE2 A:HIS310 2.1 17.7 1.0
OE2 A:GLU329 2.2 20.3 1.0
OE1 A:GLU329 2.6 23.6 1.0
CD A:GLU329 2.7 22.3 1.0
CD2 A:HIS310 2.9 15.2 1.0
CD2 A:HIS306 3.0 15.2 1.0
CE1 A:HIS306 3.0 17.0 1.0
CE1 A:HIS310 3.1 18.3 1.0
O A:HOH1035 3.7 31.2 1.0
OE1 A:GLU275 3.9 19.5 1.0
O A:HOH1117 4.1 41.5 1.0
ND1 A:HIS306 4.1 16.8 1.0
CG A:HIS306 4.1 14.2 1.0
CG A:HIS310 4.1 14.1 1.0
CG A:GLU329 4.1 13.2 1.0
ND1 A:HIS310 4.2 15.5 1.0
CB A:ALA332 4.3 14.5 1.0
OE1 A:GLU307 4.3 21.1 1.0
O A:HOH1028 4.3 24.8 1.0
CA A:GLU329 4.3 15.7 1.0
CD A:GLU275 4.4 21.0 1.0
O A:HOH1258 4.4 30.2 1.0
OE2 A:GLU275 4.4 23.3 1.0
CB A:GLU329 4.6 15.7 1.0
OE2 A:GLU307 4.7 25.6 1.0
O A:HOH1603 4.7 49.1 1.0
O A:ASN328 4.9 14.2 1.0
CD A:GLU307 4.9 25.4 1.0
N A:GLU329 5.0 12.7 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: Fri Aug 22 05:37:36 2025

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