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PDBsum entry 3se0

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protein ligands links
Hydrolase PDB id
3se0
Jmol PyMol
Contents
Protein chain
519 a.a.
Ligands
SO4
ACY ×2
MPD ×3
TRS
Waters ×143
PDB id:
3se0
Name: Hydrolase
Title: Structural characterization of the subunit a mutant f508w of synthase from pyrococcus horikoshii
Structure: V-type atp synthase alpha chain. Chain: a. Fragment: unp residues 1-240, 617-964. Synonym: a-type atp synthase catalytic subunit a, v-atpase engineered: yes. Mutation: yes. Other_details: the fusion protein of residues 1-240 and 617 atpase subunit a
Source: Pyrococcus horikoshii. Organism_taxid: 70601. Strain: ot3. Gene: atpa, ph1975. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
2.62Å     R-factor:   0.227     R-free:   0.272
Authors: V.S.Tadwal,M.S.S.Manimekalai,A.M.Balakrishna,G.Gruber
Key ref: V.S.Tadwal et al. (2011). Engineered tryptophan in the adenine-binding pocket of catalytic subunit A of A-ATP synthase demonstrates the importance of aromatic residues in adenine binding, forming a tool for steady-state and time-resolved fluorescence spectroscopy. Acta Crystallogr Sect F Struct Biol Cryst Commun, 67, 1485-1491. PubMed id: 22139149 DOI: 10.1107/S1744309111039595
Date:
09-Jun-11     Release date:   25-Jan-12    
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.
519 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 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   3 terms 
  Biochemical function     hydrolase activity, acting on acid anhydrides, catalyzing transmembrane movement of substances     2 terms  

 

 
    reference    
 
 
DOI no: 10.1107/S1744309111039595 Acta Crystallogr Sect F Struct Biol Cryst Commun 67:1485-1491 (2011)
PubMed id: 22139149  
 
 
Engineered tryptophan in the adenine-binding pocket of catalytic subunit A of A-ATP synthase demonstrates the importance of aromatic residues in adenine binding, forming a tool for steady-state and time-resolved fluorescence spectroscopy.
V.S.Tadwal, M.S.Manimekalai, G.Grüber.
 
  ABSTRACT  
 
No abstract given.

 

 

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