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Atomistry » Calcium » PDB 7uww-7vmj » 7v9n | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Calcium » PDB 7uww-7vmj » 7v9n » |
Calcium in PDB 7v9n: Crystal Structure of the Lanthipeptide Zinc-Metallopeptidase Eryp From Saccharopolyspora Erythraea in Closed StateEnzymatic 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:
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 Binding Sites:
The binding sites of Calcium 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 Calcium atom.
In total only one binding site of Calcium was determined in the Crystal Structure of the Lanthipeptide Zinc-Metallopeptidase Eryp From Saccharopolyspora Erythraea in Closed State, PDB code: 7v9n: Calcium binding site 1 out of 1 in 7v9nGo back to![]() ![]()
Calcium 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
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.
Page generated: Fri Jul 19 05:17:59 2024
ISSN: ESSN 1552-4469 PubMed: 35513512 DOI: 10.1038/S41589-022-01018-2 |
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