4XX0
CoA bound to pig GTP-specific succinyl-CoA synthetase
Summary for 4XX0
| Entry DOI | 10.2210/pdb4xx0/pdb |
| Related | 1EUC 1EUD 2FP4 2FPG 2FPI 2FPP |
| Descriptor | Succinyl-CoA ligase [ADP/GDP-forming] subunit alpha, mitochondrial, Succinyl-CoA ligase [GDP-forming] subunit beta, mitochondrial, COENZYME A, ... (7 entities in total) |
| Functional Keywords | ligase, atp-grasp fold |
| Biological source | Sus scrofa (Pig) More |
| Total number of polymer chains | 2 |
| Total formula weight | 77558.05 |
| Authors | Fraser, M.E.,Huang, J.,Malhi, M. (deposition date: 2015-01-29, release date: 2015-08-12, Last modification date: 2024-11-13) |
| Primary citation | Huang, J.,Malhi, M.,Deneke, J.,Fraser, M.E. Structure of GTP-specific succinyl-CoA synthetase in complex with CoA. Acta Crystallogr.,Sect.F, 71:1067-1071, 2015 Cited by PubMed Abstract: Pig GTP-specific succinyl-CoA synthetase is an αβ-heterodimer. The crystal structure of the complex with the substrate CoA was determined at 2.1 Å resolution. The structure shows CoA bound to the amino-terminal domain of the α-subunit, with the free thiol extending from the adenine portion into the site where the catalytic histidine residue resides. PubMed: 26249701DOI: 10.1107/S2053230X15011188 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
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