1cqj Summary

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CRYSTAL STRUCTURE OF DEPHOSPHORYLATED E. COLI SUCCINYL-COA SYNTHETASE

The structure was published by Joyce, M.A., Fraser, M.E., James, M.N., Bridger, W.A., and Wolodko, W.T., in 2000 in a paper entitled "ADP-binding site of Escherichia coli succinyl-CoA synthetase revealed by x-ray crystallography." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.9 Å and deposited in 1999.

The experimental data on which the structure is based was also deposited.

This PDB entry contains a complex of 2 biomacromolecules, namely SUCCINYL-COA SYNTHETASE ALPHA CHAIN and SUCCINYL-COA SYNTHETASE BETA CHAIN.

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 heterotetramers.

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 SUCCINYL-COA SYNTHETASE ALPHA CHAIN P0AGE9 (2-287) (SUCD_ECOLI)search Escherichia coli K-12search 99% 286 100%
D SUCCINYL-COA SYNTHETASE ALPHA CHAIN P0AGE9 (2-287) (SUCD_ECOLI)search Escherichia coli K-12search 99% 286 100%
B SUCCINYL-COA SYNTHETASE BETA CHAIN P0A836 (1-385) (SUCC_ECOLI)search Escherichia coli K-12search 99% 385 100%
E SUCCINYL-COA SYNTHETASE BETA CHAIN P0A836 (1-385) (SUCC_ECOLI)search Escherichia coli K-12search 99% 385 100%


This entry contains 2 unique UniProt proteins:

UniProt accession Name Organism PDB
P0AGE9 (2 - 287) SUCCINYL-COA SYNTHETASE ALPHA CHAIN Escherichia coli
P0A836 (1 - 385) SUCCINYL-COA SYNTHETASE BETA CHAIN Escherichia coli

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A, D (P0AGE9) CoA-binding domainsearch, Succinyl-CoA synthetase domainssearch NAD(P)-binding Rossmann-like Domainsearch, Rossmann foldsearch PF00549: CoA-ligasesearch, PF02629: CoA binding domainsearch
B, E (P0A836) Succinyl-CoA synthetase domainssearch, Succinyl-CoA synthetase, beta-chain, N-terminal domainsearch ATP-grasp fold, B domainsearch, ATP-grasp fold, A domainsearch, Rossmann foldsearch PF00549: CoA-ligasesearch, PF08442: ATP-grasp domainsearch

Chain ID Biological process (GO) Molecular function (GO) Cellular component (GO)
A, D (P0AGE9) protein autophosphorylationsearch metabolic processsearch tricarboxylic acid cyclesearch ligase activitysearch protein bindingsearch catalytic activitysearch succinate-CoA ligase (ADP-forming) activitysearch ATP citrate synthase activitysearch cofactor bindingsearch nucleotide bindingsearch ATP bindingsearch cytoplasmsearch succinate-CoA ligase complex (ADP-forming)search
B, E (P0A836) metabolic processsearch tricarboxylic acid cyclesearch catalytic activitysearch ligase activitysearch protein bindingsearch metal ion bindingsearch ATP bindingsearch manganese ion bindingsearch succinate-CoA ligase (ADP-forming) activitysearch nucleotide bindingsearch magnesium ion bindingsearch succinate-CoA ligase complex (ADP-forming)search cytoplasmsearch

Chain InterPro annotation
A, D CoA-bindingsearch Succinyl-CoA ligase, alpha subunitsearch ATP-citrate lyase/succinyl-CoA ligasesearch NAD(P)-binding domainsearch Succinyl-CoA synthetase-likesearch ATP-citrate lyase/succinyl-CoA ligase, active sitesearch
B, E Succinyl-CoA synthetase, beta subunitsearch ATP-citrate lyase/succinyl-CoA ligasesearch ATP-grasp foldsearch ATP-grasp fold, succinyl-CoA synthetase-typesearch ATP-grasp fold, subdomain 1search ATP-grasp fold, subdomain 2search Succinyl-CoA synthetase-likesearch Succinyl-CoA synthetase, beta subunit, conserved sitesearch