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PDBsum entry 3ezn

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protein ligands Protein-protein interface(s) links
Isomerase PDB id
3ezn

 

 

 

 

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JSmol PyMol  
Contents
Protein chains
236 a.a. *
Ligands
PG4 ×4
Waters ×365
* Residue conservation analysis
PDB id:
3ezn
Name: Isomerase
Title: Crystal structure of phosphoglyceromutase from burkholderia pseudomallei 1710b
Structure: 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase. Chain: a, b. Synonym: phosphoglyceromutase, pgam, bpg-dependent pgam, dpgm. Engineered: yes
Source: Burkholderia pseudomallei 1710b. Organism_taxid: 320372. Strain: 1719b. Gene: gpma, burps1710b_0662. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
2.10Å     R-factor:   0.152     R-free:   0.204
Authors: Seattle Structural Genomics Center For Infectious Disease (Ssgcid)
Key ref: D.R.Davies et al. (2011). An ensemble of structures of Burkholderia pseudomallei 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase. Acta Crystallogr Sect F Struct Biol Cryst Commun, 67, 1044-1050. PubMed id: 21904048
Date:
23-Oct-08     Release date:   11-Nov-08    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
Q3JWH7  (GPMA_BURP1) -  2,3-bisphosphoglycerate-dependent phosphoglycerate mutase from Burkholderia pseudomallei (strain 1710b)
Seq:
Struc:
249 a.a.
236 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.5.4.2.11  - phosphoglycerate mutase (2,3-diphosphoglycerate-dependent).
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: (2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate
2-phospho-D-glycerate
= 3-phospho-D-glycerate
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

 
    Added reference    
 
 
Acta Crystallogr Sect F Struct Biol Cryst Commun 67:1044-1050 (2011)
PubMed id: 21904048  
 
 
An ensemble of structures of Burkholderia pseudomallei 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase.
D.R.Davies, B.L.Staker, J.A.Abendroth, T.E.Edwards, R.Hartley, J.Leonard, H.Kim, A.L.Rychel, S.N.Hewitt, P.J.Myler, L.J.Stewart.
 
  ABSTRACT  
 
No abstract given.

 

 

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