2fp4 Summary

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Crystal structure of pig GTP-specific succinyl-CoA synthetase in complex with GTP

The structure was published by Fraser, M.E., Hayakawa, K., Hume, M.S., Ryan, D.G., and Brownie, E.R., in 2006 in a paper entitled "Interactions of GTP with the ATP-grasp Domain of GTP-specific Succinyl-CoA Synthetase" (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.08 Å and deposited in 2006.

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

This PDB entry contains a complex of 2 biomacromolecules, namely Succinyl-CoA ligase [GDP-forming] alpha-chain, mitochondrial and Succinyl-CoA ligase [GDP-forming] beta-chain, mitochondrial.

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 heterodimers.

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 ligase [GDP-forming] alpha-chain, mitochondrial O19069 (43-346) (SUCA_PIG)search Sus scrofasearch < 90% 305 100%
B Succinyl-CoA ligase [GDP-forming] beta-chain, mitochondrial P53590 (40-433) (SUCB2_PIG)search Sus scrofasearch 91% 395 99%


This entry contains 2 unique UniProt proteins:

UniProt accession Name Organism PDB
O19069 (43 - 346) Succinyl-CoA ligase [GDP-forming] alpha-chain, mitochondrial Sus scrofa
P53590 (40 - 433) Succinyl-CoA ligase [GDP-forming] beta-chain, mitochondrial Sus scrofa

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A CoA-binding domainsearch, Succinyl-CoA synthetase domainssearch NAD(P)-binding Rossmann-like Domainsearch, Rossmann foldsearch CoA-ligasesearch, CoA binding domainsearch
B (P53590) 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 Molecular function (GO) Biological process (GO) Cellular component (GO)
A (O19069) ATP citrate synthase activitysearch catalytic activitysearch cofactor bindingsearch succinate-CoA ligase (ADP-forming) activitysearch metabolic processsearch
B (P53590) catalytic activitysearch GTP bindingsearch ligase activitysearch nucleotide bindingsearch succinate-CoA ligase (GDP-forming) activitysearch ATP bindingsearch metabolic processsearch tricarboxylic acid cyclesearch mitochondrionsearch

Chain InterPro annotation
A 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 Succinyl-CoA synthetase, beta subunitsearch ATP-citrate lyase/succinyl-CoA ligasesearch 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