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PDBsum entry 3idh

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protein ligands metals links
Transferase PDB id
3idh
Jmol
Contents
Protein chain
453 a.a. *
Ligands
GLC
Metals
__K
Waters ×225
* Residue conservation analysis
PDB id:
3idh
Name: Transferase
Title: Human pancreatic glucokinase in complex with glucose
Structure: Glucokinase. Chain: a. Fragment: unp residues 12-465. Synonym: hexokinase type iv, hk iv, hexokinase-4, hk4, hexo engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
2.14Å     R-factor:   0.190     R-free:   0.220
Authors: P.Petit,L.Gluais,A.Lagarde,J.A.Boutin,G.Ferry,L.Vuillard
Key ref: P.Petit et al. (2011). The active conformation of human glucokinase is not altered by allosteric activators. Acta Crystallogr D Biol Crystallogr, 67, 929-935. PubMed id: 22101819 DOI: 10.1107/S0907444911036729
Date:
21-Jul-09     Release date:   28-Jul-10    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P35557  (HXK4_HUMAN) -  Glucokinase
Seq:
Struc:
465 a.a.
453 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 7 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class: E.C.2.7.1.2  - Glucokinase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: ATP + D-glucose = ADP + D-glucose 6-phosphate
ATP
+
D-glucose
Bound ligand (Het Group name = GLC)
corresponds exactly
= ADP
+ D-glucose 6-phosphate
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     cytoplasm   7 terms 
  Biological process     metabolic process   35 terms 
  Biochemical function     catalytic activity     15 terms  

 

 
    reference    
 
 
DOI no: 10.1107/S0907444911036729 Acta Crystallogr D Biol Crystallogr 67:929-935 (2011)
PubMed id: 22101819  
 
 
The active conformation of human glucokinase is not altered by allosteric activators.
P.Petit, M.Antoine, G.Ferry, J.A.Boutin, A.Lagarde, L.Gluais, R.Vincentelli, L.Vuillard.
 
  ABSTRACT  
 
No abstract given.