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PDBsum entry 4ear

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protein ligands Protein-protein interface(s) links
Transferase/transferase inhibitor PDB id
4ear
Jmol
Contents
Protein chain
283 a.a.
Ligands
IM5 ×3
PO4 ×3
Waters ×579
PDB id:
4ear
Name: Transferase/transferase inhibitor
Title: Crystal structure of purine nucleoside phosphorylase (w16y, w178y, h257w) mutant from human complexed with dadme-immg a phosphate
Structure: Purine nucleoside phosphorylase. Chain: a, b, c. Synonym: pnp, inosine phosphorylase. Engineered: yes. Mutation: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: np, pnp, x00737.1. Expressed in: escherichia coli. Expression_system_taxid: 469008.
Resolution:
1.70Å     R-factor:   0.176     R-free:   0.203
Authors: A.M.Haapalainen,M.C.Ho,J.J.Suarez,S.C.Almo,V.L.Schramm
Key ref: J.Suarez et al. (2013). Catalytic site conformations in human PNP by 19F-NMR and crystallography. Chem Biol, 20, 212-222. PubMed id: 23438750 DOI: 10.1016/j.chembiol.2013.01.009
Date:
22-Mar-12     Release date:   06-Feb-13    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P00491  (PNPH_HUMAN) -  Purine nucleoside phosphorylase
Seq:
Struc:
289 a.a.
283 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 5 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class: E.C.2.4.2.1  - Purine-nucleoside phosphorylase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction:
1. Purine nucleoside + phosphate = purine + alpha-D-ribose 1-phosphate
2. Purine deoxynucleoside + phosphate = purine + 2'-deoxy-alpha-D-ribose 1-phosphate
Purine nucleoside
Bound ligand (Het Group name = IM5)
matches with 58.33% similarity
+
phosphate
Bound ligand (Het Group name = PO4)
corresponds exactly
= purine
+ alpha-D-ribose 1-phosphate
Purine deoxynucleoside
+ phosphate
= purine
+ 2'-deoxy-alpha-D-ribose 1-phosphate
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     intracellular   5 terms 
  Biological process     small molecule metabolic process   16 terms 
  Biochemical function     catalytic activity     9 terms  

 

 
    reference    
 
 
DOI no: 10.1016/j.chembiol.2013.01.009 Chem Biol 20:212-222 (2013)
PubMed id: 23438750  
 
 
Catalytic site conformations in human PNP by 19F-NMR and crystallography.
J.Suarez, A.M.Haapalainen, S.M.Cahill, M.C.Ho, F.Yan, S.C.Almo, V.L.Schramm.
 
  ABSTRACT  
 
No abstract given.