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PDBsum entry 3qg1

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protein ligands links
Hydrolase PDB id
3qg1
Jmol
Contents
Protein chain
561 a.a.
Ligands
ACY ×6
MPD ×3
Waters ×33
PDB id:
3qg1
Name: Hydrolase
Title: Crystal structure of p-loop g239a mutant of subunit a of the synthase
Structure: V-type atp synthase alpha chain. Chain: a. Fragment: catalytic subunit a (unp residues 1-240, 617-964) synonym: a-type atp synthase catalytic subunit a, v-atpase engineered: yes. Mutation: yes
Source: Pyrococcus horikoshii. Organism_taxid: 70601. Strain: ot3. Gene: atpa, ph1975. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
2.95Å     R-factor:   0.265     R-free:   0.319
Authors: P.Ragunathan,M.S.S.Manimekalai,A.Kumar,J.Jeyakanthan,G.Grube
Key ref: R.Priya et al. (2011). Conserved glycine residues in the P-loop of ATP synthases form a doorframe for nucleotide entrance. J Mol Biol, 413, 657-666. PubMed id: 21925186
Date:
24-Jan-11     Release date:   05-Oct-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.
561 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 413:657-666 (2011)
PubMed id: 21925186  
 
 
Conserved glycine residues in the P-loop of ATP synthases form a doorframe for nucleotide entrance.
R.Priya, A.Kumar, M.S.Manimekalai, G.Grüber.
 
  ABSTRACT  
 
No abstract given.