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Hydrolase PDB-id
1yvw
Biological unit* = asymmetric unit,
as shown
(*as deduced by PQS)
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Description
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Protein chains
92 a.a. *
Waters ×169

* Residue conservation analysis
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PDB id: 1yvw
Name: Hydrolase
Title: Crystal structure of phosphoribosyl-atp pyrophosphohydrolase from bacillus cereus. Nesgc target bcr13.

Structure:
Phosphoribosyl-atp pyrophosphatase. Chain: a, b, c, d. Synonym: pra-ph. Engineered: yes

Source:
Bacillus cereus. Organism_taxid: 1396. Atcc: 14579. Gene: hise. Expressed in: escherichia coli. Expression_system_taxid: 562

Biological unit:
Tetramer (from PQS)

UniProt:
Chains A, B, C, D: Q81G00 (HIS2_BACCR)
Pfam  
Seq: 107 a.a.
Struc: 92 a.a.
Key:    PfamA domain
 Secondary structure  CATH domain

Enzyme class:
E.C.3.6.1.31   [IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

Reaction:
1-(5-phosphoribosyl)-ATP + H2O = 1-(5-phosphoribosyl)-AMP + diphosphate (see diagram below)

Pathway:
Histidine Biosynthesis (early stages)

Resolution:
2.60Å

R-factor:
0.244

R-free:
0.263

Authors:
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)

Key ref:
j.benach et al. Crystal structure of Phosphoribosyl-ATP pyrophosphohydrolase from Bacillus cereus at 2.6 A resolution.. To be Published, xsi:nil="true" />.

Date:
16-Feb-05

Release date:
01-Mar-05

Related entries:
Bcr13 related db: targetdb
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Enzyme reaction for E.C.3.6.1.31


1-(5-phosphoribosyl)-ATP
+ H(2)O
=
1-(5-phosphoribosyl)-AMP
+
diphosphate
Molecule diagrams generated from .mol files obtained from the KEGG ftp site.