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PDBsum entry 3b6r

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protein ligands metals Protein-protein interface(s) links
Transferase PDB id
3b6r
Jmol
Contents
Protein chain
376 a.a. *
Ligands
ACT ×2
NO3
ADP
CRN
Metals
_MG
Waters ×586
* Residue conservation analysis
PDB id:
3b6r
Name: Transferase
Title: Crystal structure of human brain-type creatine kinase
Structure: Creatine kinase b-type. Chain: a, b. Synonym: creatine kinase b chain, b-ck. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: ckb. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
2.00Å     R-factor:   0.192     R-free:   0.231
Authors: S.M.Bong,J.H.Moon,K.Y.Hwang
Key ref: S.M.Bong et al. (2008). Structural studies of human brain-type creatine kinase complexed with the ADP-Mg2+-NO3- -creatine transition-state analogue complex. FEBS Lett, 582, 3959-3965. PubMed id: 18977227 DOI: 10.1016/j.febslet.2008.10.039
Date:
29-Oct-07     Release date:   04-Nov-08    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P12277  (KCRB_HUMAN) -  Creatine kinase B-type
Seq:
Struc:
381 a.a.
376 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.2.7.3.2  - Creatine kinase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

      Pathway:
Creatine Biosynthesis
      Reaction: ATP + creatine = ADP + phosphocreatine
ATP
+
creatine
Bound ligand (Het Group name = CRN)
corresponds exactly
=
ADP
Bound ligand (Het Group name = ADP)
corresponds exactly
+ phosphocreatine
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     cytoplasm   4 terms 
  Biological process     small molecule metabolic process   7 terms 
  Biochemical function     catalytic activity     8 terms  

 

 
    reference    
 
 
DOI no: 10.1016/j.febslet.2008.10.039 FEBS Lett 582:3959-3965 (2008)
PubMed id: 18977227  
 
 
Structural studies of human brain-type creatine kinase complexed with the ADP-Mg2+-NO3- -creatine transition-state analogue complex.
S.M.Bong, J.H.Moon, K.H.Nam, K.S.Lee, Y.M.Chi, K.Y.Hwang.
 
  ABSTRACT  
 
Creatine kinase is a member of the phosphagen kinase family, which catalyzes the reversible phosphoryl transfer reaction that occurs between ATP and creatine to produce ADP and phosphocreatine. Here, three structural aspects of human-brain-type-creatine-kinase (hBB-CK) were identified by X-ray crystallography: the ligand-free-form at 2.2A; the ADP-Mg2+, nitrate, and creatine complex (transition-state-analogue complex; TSAC); and the ADP-Mg2+-complex at 2.0A. The structures of ligand-bound hBB-CK revealed two different monomeric states in a single homodimer. One monomer is a closed form, either bound to TSAC or the ADP-Mg2+-complex, and the second monomer is an unliganded open form. These structural studies provide a detailed mechanism indicating that the binding of ADP-Mg2+ alone may trigger conformational changes in hBB-CK that were not observed with muscle-type-CK.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
21507330 N.Liu, J.S.Wang, W.D.Wang, and J.C.Pan (2011).
The role of Cys271 in conformational changes of arginine kinase.
  Int J Biol Macromol, 49, 98.  
21036862 Q.Xu, and R.L.Dunbrack (2011).
The protein common interface database (ProtCID)--a comprehensive database of interactions of homologous proteins in multiple crystal forms.
  Nucleic Acids Res, 39, D761-D770.  
20717523 Y.S.Gao, J.T.Su, and Y.B.Yan (2010).
Sequential events in the irreversible thermal denaturation of human brain-type creatine kinase by spectroscopic methods.
  Int J Mol Sci, 11, 2584-2596.  
20057941 Q.Sheng, H.C.Zou, Z.R.Lü, F.Zou, Y.D.Park, Y.B.Yan, and S.J.Yao (2009).
Effects of acrylamide on the activity and structure of human brain creatine kinase.
  Int J Mol Sci, 10, 4210-4222.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time.