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Biological unit* = asymmetric unit,
as shown
(*as deduced by
)
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*
Residue conservation analysis
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| PDB id: |
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1yvw
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| Name: |
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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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Biological unit:
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Tetramer (from
)
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UniProt:
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Chains A,
B,
C,
D:
Q81G00
(HIS2_BACCR)
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| Seq: |
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107 a.a. |
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| Struc: |
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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Reaction:
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1-(5-phosphoribosyl)-ATP + H2O = 1-(5-phosphoribosyl)-AMP + diphosphate
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Pathway:
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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,
xsi:nil="true" />.
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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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Related entries:
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Bcr13 related db: targetdb
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Quick_links |
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