PDBsum entry 1g0w

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protein ligands links
Transferase PDB id
Protein chain
372 a.a. *
SO4 ×2
Waters ×72
* Residue conservation analysis
PDB id:
Name: Transferase
Title: Crystal structure of bovine retinal creatine kinase
Structure: Creatine kinase. Chain: a. Ec:
Source: Bos taurus. Cattle. Organism_taxid: 9913. Organ: retina
Biol. unit: Dimer (from PQS)
2.30Å     R-factor:   0.197     R-free:   0.232
Authors: D.Tisi,B.Bax,A.Loew
Key ref:
D.Tisi et al. (2001). The three-dimensional structure of cytosolic bovine retinal creatine kinase. Acta Crystallogr D Biol Crystallogr, 57, 187-193. PubMed id: 11173463 DOI: 10.1107/S0907444900015614
09-Oct-00     Release date:   07-Feb-01    
Go to PROCHECK summary

Protein chain
Pfam   ArchSchema ?
Q9XSC6  (KCRM_BOVIN) -  Creatine kinase M-type
381 a.a.
372 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 75 residue positions (black crosses)

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

Creatine Biosynthesis
      Reaction: ATP + creatine = ADP + phosphocreatine
+ creatine
+ phosphocreatine
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     cytoplasm   1 term 
  Biological process     phosphorylation   2 terms 
  Biochemical function     catalytic activity     7 terms  


DOI no: 10.1107/S0907444900015614 Acta Crystallogr D Biol Crystallogr 57:187-193 (2001)
PubMed id: 11173463  
The three-dimensional structure of cytosolic bovine retinal creatine kinase.
D.Tisi, B.Bax, A.Loew.
Creatine kinase (CK) catalyses the reversible transfer of the phosphate moiety from phosphocreatine (PCr) to ADP, generating creatine and ATP. The crystal structure of a cytosolic brain-type creatine kinase is reported at 2.3 A. The biological dimer sits on a crystallographic twofold axis. The N-terminal residues of both subunits come very close to the crystallographic twofold at the dimer interface. The electron density observed is consistent with two alternative conformations for the N-termini, as previously found for chicken brain-type creatine kinase.
  Selected figure(s)  
Figure 4.
Figure 4 Structure of the brB-CK dimer. The dimer is composed of two monomers related by a twofold rotation axis (perpendicular to the plane of the paper). The dimer interface is formed mainly by four regions ( 1/ 7 and loop207-210/ 4) as described in detail in the text. The first 11 amino acids of each monomer are tentatively build into density with an occupancy of 0.5.
Figure 5.
Figure 5 Alignment of sequences of bovine retinal brain-type creatine kinase (brB-CK), chicken mitochondrial CK (cMi-CK), human ubiquitous mitochondrial CK (uMi-CK), rabbit muscle CK (rM-CK), chicken brain-type CK (chB-CK) and horseshoe crab arginine kinase (hc-AK). -Helices are represented as cylinders and -strands are shown as green arrows. Highlighted in blue are residues making contacts across the brB-CK and the cMi-CK dimer interface (distances less than 4 ). Residues in red are amino acids with distances less then 4 of transition-state analogue substrate in horseshoe crab arginine kinase.
  The above figures are reprinted by permission from the IUCr: Acta Crystallogr D Biol Crystallogr (2001, 57, 187-193) copyright 2001.  
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
  18765922 A.M.Awama, P.Paracuellos, S.Laurent, C.Dissous, O.Marcillat, and P.Gouet (2008).
Crystallization and X-ray analysis of the Schistosoma mansoni guanidino kinase.
  Acta Crystallogr Sect F Struct Biol Cryst Commun, 64, 854-857.  
14739330 H.Mazon, O.Marcillat, E.Forest, and C.Vial (2004).
Hydrogen/deuterium exchange studies of native rabbit MM-CK dynamics.
  Protein Sci, 13, 476-486.  
12592023 C.L.Borders, K.M.MacGregor, P.L.Edmiston, E.R.Gbeddy, M.J.Thomenius, G.B.Mulligan, and M.J.Snider (2003).
Asparagine 285 plays a key role in transition state stabilization in rabbit muscle creatine kinase.
  Protein Sci, 12, 532-537.  
12493833 M.S.Yousef, S.A.Clark, P.K.Pruett, T.Somasundaram, W.R.Ellington, and M.S.Chapman (2003).
Induced fit in guanidino kinases--comparison of substrate-free and transition state analog structures of arginine kinase.
  Protein Sci, 12, 103-111.
PDB code: 1m80
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