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PDBsum entry 2y33

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protein ligands metals links
Oxidoreductase PDB id
2y33
Jmol
Contents
Protein chain
216 a.a. *
Ligands
UN9
Metals
_ZN
Waters ×143
* Residue conservation analysis
PDB id:
2y33
Name: Oxidoreductase
Title: S-nitrosylated phd2 (gsno soaked) in complex with zn(ii) and
Structure: Egl nine homolog 1. Chain: a. Fragment: catalytic domain, residues 181-426. Synonym: hypoxia-inducible factor prolyl hydroxylase 2, pro hydroxylase domain-containing protein 2, sm-20, hif-ph2, hif-prolyl hydroxylase 2, hph-2, phd2. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 469008.
Resolution:
2.00Å     R-factor:   0.209     R-free:   0.246
Authors: R.Chowdhury,I.J.Clifton,C.J.Schofield
Key ref: R.Chowdhury et al. (2011). Studies on the reaction of nitric oxide with the hypoxia-inducible factor prolyl hydroxylase domain 2 (EGLN1). J Mol Biol, 410, 268-279. PubMed id: 21601578 DOI: 10.1016/j.jmb.2011.04.075
Date:
18-Dec-10     Release date:   29-Dec-10    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
Q9GZT9  (EGLN1_HUMAN) -  Egl nine homolog 1
Seq:
Struc:
426 a.a.
216 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 Enzyme reactions 
   Enzyme class: E.C.1.14.11.29  - Hypoxia-inducible factor-proline dioxygenase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Hypoxia-inducible factor-L-proline + 2-oxoglutarate + O2 = hypoxia- inducible factor-trans-4-hydroxy-L-proline + succinate + CO2
Hypoxia-inducible factor-L-proline
+ 2-oxoglutarate
+ O(2)
= hypoxia- inducible factor-trans-4-hydroxy-L-proline
+ succinate
+ CO(2)
      Cofactor: Iron; L-ascorbate
Iron
L-ascorbate
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     oxidation-reduction process   1 term 
  Biochemical function     oxidoreductase activity     5 terms  

 

 
    reference    
 
 
DOI no: 10.1016/j.jmb.2011.04.075 J Mol Biol 410:268-279 (2011)
PubMed id: 21601578  
 
 
Studies on the reaction of nitric oxide with the hypoxia-inducible factor prolyl hydroxylase domain 2 (EGLN1).
R.Chowdhury, E.Flashman, J.Mecinović, H.B.Kramer, B.M.Kessler, Y.M.Frapart, J.L.Boucher, I.J.Clifton, M.A.McDonough, C.J.Schofield.
 
  ABSTRACT  
 
No abstract given.