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Contents |
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* Residue conservation analysis
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PDB id:
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Hydrolase
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Title:
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Crystal structure of phosphoribosyl-atp pyrophosphohydrolase from bacillus cereus. Nesgc target bcr13.
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Structure:
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Phosphoribosyl-atp pyrophosphatase. Chain: a, b, c, d. Synonym: pra-ph. Engineered: yes
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Source:
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Bacillus cereus. Organism_taxid: 1396. Atcc: 14579. Gene: hise. Expressed in: escherichia coli. Expression_system_taxid: 562
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Biol. unit:
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Tetramer (from
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Resolution:
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2.60Å
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R-factor:
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0.244
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R-free:
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0.263
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Authors:
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J.Benach,A.P.Kuzin,F.Forouhar,M.Abashidze,S.M.Vorobiev, R.Shastry,X.Rong,T.B.Acton,G.T.Montelione,J.F.Hunt, Northeast Structural Genomics Consortium (Nesg)
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Key ref:
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J.Benach
et al.
Crystal structure of phosphoribosyl-Atp pyrophosphohydrolase from bacillus cereus at 2.6 a resolution..
To be published,
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Date:
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16-Feb-05
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Release date:
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01-Mar-05
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PROCHECK
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Headers
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References
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Q81G00
(HIS2_BACCR) -
Phosphoribosyl-ATP pyrophosphatase
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Seq:
Struc:
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107 a.a.
92 a.a.
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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Enzyme class:
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E.C.3.6.1.31
- Phosphoribosyl-ATP diphosphatase.
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Pathway:
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Histidine Biosynthesis (early stages)
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Reaction:
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1-(5-phosphoribosyl)-ATP + H2O = 1-(5-phosphoribosyl)-AMP + diphosphate
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1-(5-phosphoribosyl)-ATP
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+
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H(2)O
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=
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1-(5-phosphoribosyl)-AMP
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+
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diphosphate
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Molecule diagrams generated from .mol files obtained from the
KEGG ftp site
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Gene Ontology (GO) functional annotation
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Cellular component
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cytoplasm
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1 term
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Biological process
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cellular amino acid biosynthetic process
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2 terms
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Biochemical function
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nucleotide binding
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4 terms
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Links
