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PDBsum entry 2d33
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Contents |
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* Residue conservation analysis
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PDB id:
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| Name: |
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Ligase
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Title:
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Crystal structure of gamma-glutamylcysteine synthetase complexed with aluminum fluoride
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Structure:
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Glutamate--cysteine ligase. Chain: a, b, c, d. Synonym: gamma-glutamylcysteine synthetase, gamma-ecs, gcs. Engineered: yes. Mutation: yes
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Source:
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Escherichia coli. Organism_taxid: 562. Gene: gshi. 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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0.164
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R-free:
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0.191
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Authors:
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T.Hibi,M.Nakayama,H.Nii,Y.Kurokawa,H.Katano,J.Oda
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Key ref:
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T.Hibi
et al.
Structural basis of efficient coupling between peptide ligation and ATP hydrolysis by gamma-Gluatamylcysteine synthetase.
To be published,
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Date:
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25-Sep-05
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Release date:
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14-Nov-06
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PROCHECK
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Headers
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References
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P0A6W9
(GSH1_ECOLI) -
Glutamate--cysteine ligase from Escherichia coli (strain K12)
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Seq:
Struc:
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518 a.a.
510 a.a.*
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Key: |
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PfamA domain |
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Secondary structure |
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*
PDB and UniProt seqs differ
at 3 residue positions (black
crosses)
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Enzyme class:
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E.C.6.3.2.2
- glutamate--cysteine ligase.
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Reaction:
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L-cysteine + L-glutamate + ATP = gamma-L-glutamyl-L-cysteine + ADP + phosphate + H+
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L-cysteine
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+
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L-glutamate
Bound ligand (Het Group name = )
corresponds exactly
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+
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ATP
Bound ligand (Het Group name = )
corresponds exactly
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=
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gamma-L-glutamyl-L-cysteine
Bound ligand (Het Group name = )
corresponds exactly
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+
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ADP
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+
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phosphate
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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
