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PDBsum entry 1kp0

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protein Protein-protein interface(s) links
Hydrolase PDB id
1kp0
Jmol
Contents
Protein chains
402 a.a. *
Waters ×118
* Residue conservation analysis
PDB id:
1kp0
Name: Hydrolase
Title: The crystal structure analysis of creatine amidinohydrolase from actinobacillus
Structure: Creatine amidinohydrolase. Chain: a, b. Ec: 3.5.3.3
Source: Actinobacillus. Organism_taxid: 713
Biol. unit: Dimer (from PQS)
Resolution:
2.70Å     R-factor:   0.188     R-free:   0.222
Authors: B.Padmanabhan,A.Paehler,M.Horikoshi
Key ref:
B.Padmanabhan et al. (2002). Structure of creatine amidinohydrolase from Actinobacillus. Acta Crystallogr D Biol Crystallogr, 58, 1322-1328. PubMed id: 12136144 DOI: 10.1107/S0907444902010156
Date:
26-Dec-01     Release date:   31-Jul-02    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
Q7SIB5  (Q7SIB5_9PAST) -  Hydrolase
Seq:
Struc:
402 a.a.
402 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 37 residue positions (black crosses)

 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     metabolic process   1 term 
  Biochemical function     hydrolase activity     1 term  

 

 
DOI no: 10.1107/S0907444902010156 Acta Crystallogr D Biol Crystallogr 58:1322-1328 (2002)
PubMed id: 12136144  
 
 
Structure of creatine amidinohydrolase from Actinobacillus.
B.Padmanabhan, A.Paehler, M.Horikoshi.
 
  ABSTRACT  
 
The crystal structure of Actinobacillus creatine amidinohydrolase has been solved by molecular replacement. The amino-acid sequence has been derived from the crystal structure. Crystals belong to space group I222, with unit-cell parameters a = 111.26 (3), b = 113.62 (4), c = 191.65 (2) A, and contain two molecules in an asymmetric unit. The structure was refined to an R factor of 18.8% at 2.7 A resolution. The crystal structure contains a dimer of 402 residues and 118 water molecules. The protein structure is bilobal, consisting of a small N-terminal domain and a large C-terminal domain. The C-terminal domain has a pitta-bread fold, similar to that found in Pseudomonas putida creatinase, proline aminopeptidases and methionine aminopeptidase. Comparison with complex crystal structures of P. putida creatinase reveals that the enzyme activity of Actinobacillus creatinase might be similar to that of P. putida creatinase.
 
  Selected figure(s)  
 
Figure 3.
Figure 3 Ribbon diagram of dimeric arrangement of Ac. creatinase. The figure was prepared using the program MOLSCRIPT (Kraulis, 1991[Kraulis, P. J. (1991). J. Appl. Cryst. 24, 946-950.]).
Figure 6.
Figure 6 Superimposed binding sites of the Ac. creatinase (red) and the Pp. creatinase (black)-carbamyol sarcosine (cyan) complex. The figure was produced using MOLSCRIPT (Kraulis, 1991[Kraulis, P. J. (1991). J. Appl. Cryst. 24, 946-950.]).
 
  The above figures are reprinted by permission from the IUCr: Acta Crystallogr D Biol Crystallogr (2002, 58, 1322-1328) copyright 2002.  
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
20378650 M.Kirkwood, N.E.Le Brun, J.D.Todd, and A.W.Johnston (2010).
The dddP gene of Roseovarius nubinhibens encodes a novel lyase that cleaves dimethylsulfoniopropionate into acrylate plus dimethyl sulfide.
  Microbiology, 156, 1900-1906.  
18089575 A.P.VanDemark, H.Xin, L.McCullough, R.Rawlins, S.Bentley, A.Heroux, D.J.Stillman, C.P.Hill, and T.Formosa (2008).
Structural and functional analysis of the Spt16p N-terminal domain reveals overlapping roles of yFACT subunits.
  J Biol Chem, 283, 5058-5068.
PDB codes: 3bip 3biq 3bit
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