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PDBsum entry 3q3v

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protein ligands metals Protein-protein interface(s) links
Transferase PDB id
3q3v

 

 

 

 

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JSmol PyMol  
Contents
Protein chains
394 a.a. *
Ligands
FMT ×4
SO4 ×2
PGE ×2
Metals
__K ×4
Waters ×324
* Residue conservation analysis
PDB id:
3q3v
Name: Transferase
Title: Crystal structure of phosphoglycerate kinase from campylobacter jejuni.
Structure: Phosphoglycerate kinase. Chain: a, b. Engineered: yes
Source: Campylobacter jejuni subsp. Jejuni nctc 11168. Organism_taxid: 192222. Gene: cj1402c, pgk. Expressed in: escherichia coli. Expression_system_taxid: 469008.
Resolution:
2.15Å     R-factor:   0.190     R-free:   0.237
Authors: E.V.Filippova,Z.Wawrzak,O.Onopriyenko,A.Edwards,A.Savchenko, W.F.Anderson,Center For Structural Genomics Of Infectious Diseases (Csgid)
Key ref: H.Zheng et al. (2012). Crystal structures of putative phosphoglycerate kinases from B. anthracis and C. jejuni. J Struct Funct Genomics, 13, 15-26. PubMed id: 22403005
Date:
22-Dec-10     Release date:   12-Jan-11    
PROCHECK
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 Headers
 References

Protein chains
Q9PMQ5  (PGK_CAMJE) -  Phosphoglycerate kinase from Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC 11168)
Seq:
Struc:
400 a.a.
394 a.a.
Key:    Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.2.7.2.3  - phosphoglycerate kinase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

      Pathway:
Calvin Cycle (carbon fixation stages)
      Reaction: (2R)-3-phosphoglycerate + ATP = (2R)-3-phospho-glyceroyl phosphate + ADP
(2R)-3-phosphoglycerate
+ ATP
= (2R)-3-phospho-glyceroyl phosphate
+ ADP
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

 
    Added reference    
 
 
J Struct Funct Genomics 13:15-26 (2012)
PubMed id: 22403005  
 
 
Crystal structures of putative phosphoglycerate kinases from B. anthracis and C. jejuni.
H.Zheng, E.V.Filippova, K.L.Tkaczuk, P.Dworzynski, M.Chruszcz, P.J.Porebski, Z.Wawrzak, O.Onopriyenko, M.Kudritska, S.Grimshaw, A.Savchenko, W.F.Anderson, W.Minor.
 
  ABSTRACT  
 
No abstract given.

 

 

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