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PDBsum entry 2zts

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protein ligands metals Protein-protein interface(s) links
Atp-binding protein PDB id
2zts
Jmol
Contents
Protein chains
216 a.a. *
Ligands
ADP ×3
Metals
_MG ×3
Waters ×88
* Residue conservation analysis
PDB id:
2zts
Name: Atp-binding protein
Title: Crystal structure of kaic-like protein ph0186 from hyperthermophilic archaea pyrococcus horikoshii ot3
Structure: Putative uncharacterized protein ph0186. Chain: a, b, c. Engineered: yes
Source: Pyrococcus horikoshii. Organism_taxid: 53953. Strain: ot3. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
2.07Å     R-factor:   0.199     R-free:   0.250
Authors: H.Ming,K.Miyazono,M.Tanokura
Key ref:
H.J.Kang et al. (2009). Crystal structure of KaiC-like protein PH0186 from hyperthermophilic archaea Pyrococcus horikoshii OT3. Proteins, 75, 1035-1039. PubMed id: 19274727 DOI: 10.1002/prot.22367
Date:
08-Oct-08     Release date:   24-Mar-09    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
O57925  (O57925_PYRHO) -  Putative uncharacterized protein PH0186
Seq:
Struc:
251 a.a.
216 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     metabolic process   2 terms 
  Biochemical function     nucleotide binding     5 terms  

 

 
DOI no: 10.1002/prot.22367 Proteins 75:1035-1039 (2009)
PubMed id: 19274727  
 
 
Crystal structure of KaiC-like protein PH0186 from hyperthermophilic archaea Pyrococcus horikoshii OT3.
H.J.Kang, K.Kubota, H.Ming, K.Miyazono, M.Tanokura.
 
  ABSTRACT  
 
No abstract given.

 
  Selected figure(s)  
 
Figure 1.
Figure 1. Structure of PH0186. (A) Ribbon diagram of the monomer structure of PH0186. Color-coding runs from blue in the N-terminal region to red in the C-terminal region. Secondary structure assignments are labeled on the ribbon model. ADP molecules are presented by a stick model. Residues 99-117 and 183-186 are missing in the structure (shown by the dotted line). (B) The hexamer structure of PH0186. Subunits A(A ), B(B ), and C(C ) of the PH0186 hexamer are colored blue, purple, and orange, respectively. ADP molecules are presented by a stick model. The six-fold axis of the hexamer is presented by a black hexagon. (C) ADP binding manner in the hexamer structure of PH0186. Residues involved in ADP binding are presented by a stick model. The Mg^2+ ion is shown as a green ball near the phosphate group of ADP.
Figure 2.
Figure 2. Comparison with another structure. (A) Amino acid sequence alignment of PH0186 and KaiCI from Synechococcus sp. The secondary structure assignment for PH0186 is indicated by helices ( - and 3[10]-helices) and arrows ( -strands). Each protein contains Walker motifs A and B, and two catalytic carboxylate Glu residues. (B) Superposition of PH0186 (blue) and KaiCI (red). (C) The comparative electrostatic potential diagrams of PH0186 (a), and KaiCI (b). Positive and negative potentials are represented by blue and red, respectively. The maximum and the minimum values of electrostatic potentials are ±1 kT/e, respectively. Electrostatic potential of each protein was calculated using default parameters of APBS.
 
  The above figures are reprinted by permission from John Wiley & Sons, Inc.: Proteins (2009, 75, 1035-1039) copyright 2009.