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PDBsum entry 3nqx

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protein metals links
Hydrolase PDB id
3nqx

 

 

 

 

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Contents
Protein chain
299 a.a. *
Metals
_CA
_ZN
Waters ×437
* Residue conservation analysis
PDB id:
3nqx
Name: Hydrolase
Title: Crystal structure of vibriolysin mcp-02 mature enzyme, a zinc metalloprotease from m4 family
Structure: Secreted metalloprotease mcp02. Chain: a. Fragment: the catalytic domain, residues 205-510. Synonym: mcp-02. Engineered: yes
Source: Pseudoalteromonas sp.. Organism_taxid: 234831. Strain: sm9913. Expressed in: escherichia coli. Expression_system_taxid: 469008.
Resolution:
1.70Å     R-factor:   0.176     R-free:   0.217
Authors: X.Gao,J.Wang,J.-W.Wu,Y.-Z.Zhang
Key ref: X.Gao et al. (2010). Structural basis for the autoprocessing of zinc metalloproteases in the thermolysin family. Proc Natl Acad Sci U S A, 107, 17569-17574. PubMed id: 20876133
Date:
30-Jun-10     Release date:   06-Oct-10    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
A1DRD5  (A1DRD5_PSEU9) -  Secreted metalloprotease Mcp02 from Pseudoalteromonas sp. (strain SM9913)
Seq:
Struc:
 
Seq:
Struc:
727 a.a.
299 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.3.4.24.25  - vibriolysin.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Preferential cleavage of bonds with bulky hydrophobic groups in P2 and P1'.
      Cofactor: Zn(2+)

 

 
Proc Natl Acad Sci U S A 107:17569-17574 (2010)
PubMed id: 20876133  
 
 
Structural basis for the autoprocessing of zinc metalloproteases in the thermolysin family.
X.Gao, J.Wang, D.Q.Yu, F.Bian, B.B.Xie, X.L.Chen, B.C.Zhou, L.H.Lai, Z.X.Wang, J.W.Wu, Y.Z.Zhang.
 
  ABSTRACT  
 
No abstract given.

 

Literature references that cite this PDB file's key reference

  PubMed id Reference
23275160 A.Ruf, M.Stihle, J.Benz, M.Schmidt, and H.Sobek (2013).
Structure of Gentlyase, the neutral metalloprotease of Paenibacillus polymyxa.
  Acta Crystallogr D Biol Crystallogr, 69, 24-31.
PDB codes: 4b52 4ger
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB codes are shown on the right.

 

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