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PDBsum entry 1a9c
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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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Gtp cyclohydrolase i (c110s mutant) in complex with gtp
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Structure:
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Gtp cyclohydrolase i. Chain: a, b, c, d, e, f, g, h, i, j, k, l, m, n, o. Engineered: yes. Mutation: yes
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Source:
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Escherichia coli. Organism_taxid: 562. Organ: brain. Expressed in: escherichia coli. Expression_system_taxid: 562. Other_details: homologous expression
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Biol. unit:
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Homo-Decamer (from PDB file)
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Resolution:
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2.90Å
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R-factor:
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0.206
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R-free:
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0.288
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Authors:
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G.Auerbach,H.Nar,A.Bracher,A.Bacher,R.Huber
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Key ref:
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G.Auerbach
et al.
Gtp cyclohydrolase I in complex with gtp at 2.1 a resolution.
To be published,
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Date:
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04-Apr-98
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Release date:
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11-May-99
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PROCHECK
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Headers
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References
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P0A6T5
(GCH1_ECOLI) -
GTP cyclohydrolase 1 from Escherichia coli (strain K12)
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Seq:
Struc:
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222 a.a.
221 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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*
PDB and UniProt seqs differ
at 1 residue position (black
cross)
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Enzyme class:
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E.C.3.5.4.16
- Gtp cyclohydrolase i.
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Pathway:
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Folate Biosynthesis (early stages)
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Reaction:
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GTP + H2O = 7,8-dihydroneopterin 3'-triphosphate + formate + H+
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GTP
Bound ligand (Het Group name = )
corresponds exactly
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H2O
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=
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7,8-dihydroneopterin 3'-triphosphate
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+
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formate
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+
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H(+)
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Molecule diagrams generated from .mol files obtained from the
KEGG ftp site
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Links
