1gpm Summary

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ESCHERICHIA COLI GMP SYNTHETASE COMPLEXED WITH AMP AND PYROPHOSPHATE

The structure was published by Tesmer, J.J., Klem, T.J., Deras, M.L., Davisson, V.J., and Smith, J.L., in 1996 in a paper entitled "The crystal structure of GMP synthetase reveals a novel catalytic triad and is a structural paradigm for two enzyme families." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.2 Å and deposited in 1995.

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

This PDB entry contains multiple copies of the structure of GMP SYNTHETASE.

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 most likely forms homotetramers.

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 GMP SYNTHETASE P04079 (1-525) (GUAA_ECOLI)search Escherichia coli K-12search 100% 525 95%
B GMP SYNTHETASE P04079 (1-525) (GUAA_ECOLI)search Escherichia coli K-12search 100% 525 95%
C GMP SYNTHETASE P04079 (1-525) (GUAA_ECOLI)search Escherichia coli K-12search 100% 525 95%
D GMP SYNTHETASE P04079 (1-525) (GUAA_ECOLI)search Escherichia coli K-12search 100% 525 95%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P04079 (1 - 525) GMP SYNTHETASE Escherichia coli K-12

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A, B, C, D (P04079) Class I glutamine amidotransferases (GAT)search, N-type ATP pyrophosphatasessearch, GMP synthetase C-terminal dimerisation domainsearch Rossmann foldsearch, HUPssearch, GMP Synthetase; Chain A, domain 3search PF00117: Glutamine amidotransferase class-Isearch, PF00958: GMP synthase C terminal domainsearch, PF02540: NAD synthasesearch

Chain ID Molecular function (GO) Biological process (GO) Cellular component (GO)
A, B, C, D (P04079) ATP bindingsearch GMP synthase (glutamine-hydrolyzing) activitysearch pyrophosphatase activitysearch ligase activitysearch nucleotide bindingsearch GMP synthase activitysearch identical protein bindingsearch GMP biosynthetic processsearch purine nucleotide biosynthetic processsearch glutamine metabolic processsearch cytosolsearch

Chain InterPro annotation
A, B, C, D GMP synthase, C-terminalsearch GMP synthase, N-terminalsearch Rossmann-like alpha/beta/alpha sandwich foldsearch Glutamine amidotransferasesearch NAD/GMP synthasesearch GMP synthasesearch GMP synthetase ATP pyrophosphatase domainsearch Class I glutamine amidotransferase-likesearch