1gsa Summary

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STRUCTURE OF GLUTATHIONE SYNTHETASE COMPLEXED WITH ADP AND GLUTATHIONE

The structure was published by Hara, T., Kato, H., Katsube, Y., and Oda, J., in 1996 in a paper entitled "A pseudo-michaelis quaternary complex in the reverse reaction of a ligase: structure of Escherichia coli B glutathione synthetase complexed with ADP, glutathione, and sulfate at 2.0 A resolution." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.0 Å and deposited in 1995.

The experimental data on which the structure is based was not deposited.

The PDB entry contains the structure of GLUTATHIONE SYNTHETASE. This molecule has the UniProt identifier P04425 (GSHB_ECOLI)search. The sample contained 316 residues which is 100% of the natural sequence. Out of 316 residues 314 were observed and are deposited in the PDB.

It also contains one or more heterogenic compounds (e.g., ligands, co-factors, ions, modified amino acids, etc.); see here for a complete list.

The molecule has more than one probable quaternary state observed. For more details see the quaternary structure page.

The following tables show cross-reference information to other databases (to obtain a list of all PDB entries sharing the same property or classification, click on the magnifying glass icon):


Chain Name UniProt Name of source organism % of UniProt sequence present in the sample Residues in the sample molecules % of residues observed
A GLUTATHIONE SYNTHETASE P04425 (1-316) (GSHB_ECOLI)search Escherichia coli K-12search 96% 316 99%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P04425 (1 - 316) GLUTATHIONE SYNTHETASE Escherichia coli B

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A (P04425) Prokaryotic glutathione synthetase, N-terminal domainsearch, ATP-binding domain of peptide synthetasessearch Rossmann foldsearch, ATP-grasp fold, B domainsearch, ATP-grasp fold, A domainsearch PF02951: Prokaryotic glutathione synthetase, N-terminal domainsearch, PF02955: Prokaryotic glutathione synthetase, ATP-grasp domainsearch

Chain ID Molecular function (GO) Biological process (GO) Cellular component (GO)
A (P04425) catalytic activitysearch metal ion bindingsearch ATP bindingsearch glutathione synthase activitysearch nucleotide bindingsearch magnesium ion bindingsearch ligase activitysearch manganese ion bindingsearch glutathione biosynthetic processsearch cytosolsearch

Chain InterPro annotation
A Prokaryotic glutathione synthetase, N-terminalsearch Prokaryotic glutathione synthetase, ATP-bindingsearch Glutathione synthetase, prokaryoticsearch ATP-grasp foldsearch ATP-grasp fold, subdomain 1search ATP-grasp fold, subdomain 2search Pre-ATP-grasp domainsearch