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PDBsum entry 3nd9

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protein ligands links
Hydrolase PDB id
3nd9
Jmol
Contents
Protein chain
508 a.a.
Ligands
MRD ×2
Waters ×27
PDB id:
3nd9
Name: Hydrolase
Title: Structural characterization for the nucleotide binding abili subunit a of the a1ao atp synthase
Structure: V-type atp synthase alpha chain. Chain: a. Fragment: catalytic (unp residues 1-240, 617-964). Synonym: a-type atp synthase catalytic subunit a, v-atpase engineered: yes. Mutation: yes. Other_details: the fusion of residues 1-240 and residues 61 v-atpase subunit a
Source: Pyrococcus horikoshii, pyrococcus hori organism_taxid: 53953, 53953. Strain: ot3. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
3.10Å     R-factor:   0.223     R-free:   0.285
Authors: A.Kumar,J.Jeyakanthan,G.Gruber
Key ref: M.S.Manimekalai et al. (2011). The transition-like state and Pi entrance into the catalytic a subunit of the biological engine A-ATP synthase. J Mol Biol, 408, 736-754. PubMed id: 21396943
Date:
07-Jun-10     Release date:   30-Mar-11    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
O57728  (VATA_PYRHO) -  V-type ATP synthase alpha chain
Seq:
Struc:
 
Seq:
Struc:
964 a.a.
508 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 2 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class: E.C.3.6.3.14  - H(+)-transporting two-sector ATPase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: ATP + H2O + H+(In) = ADP + phosphate + H+(Out)
ATP
+ H(2)O
+ H(+)(In)
= ADP
+ phosphate
+ H(+)(Out)
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     proton-transporting two-sector ATPase complex, catalytic domain   1 term 
  Biological process     proton transport   4 terms 
  Biochemical function     hydrolase activity, acting on acid anhydrides, catalyzing transmembrane movement of substances     2 terms  

 

 
    reference    
 
 
J Mol Biol 408:736-754 (2011)
PubMed id: 21396943  
 
 
The transition-like state and Pi entrance into the catalytic a subunit of the biological engine A-ATP synthase.
M.S.Manimekalai, A.Kumar, J.Jeyakanthan, G.Grüber.
 
  ABSTRACT  
 
No abstract given.