5UQS
Crystal structure of Citrate synthase from Sus scrofa
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004108 | molecular_function | citrate (Si)-synthase activity |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0005759 | cellular_component | mitochondrial matrix |
| A | 0005975 | biological_process | carbohydrate metabolic process |
| A | 0006099 | biological_process | tricarboxylic acid cycle |
| A | 0006101 | biological_process | citrate metabolic process |
| A | 0016740 | molecular_function | transferase activity |
| A | 0036440 | molecular_function | citrate synthase activity |
| A | 0046912 | molecular_function | acyltransferase activity, acyl groups converted into alkyl on transfer |
| C | 0004108 | molecular_function | citrate (Si)-synthase activity |
| C | 0005739 | cellular_component | mitochondrion |
| C | 0005759 | cellular_component | mitochondrial matrix |
| C | 0005975 | biological_process | carbohydrate metabolic process |
| C | 0006099 | biological_process | tricarboxylic acid cycle |
| C | 0006101 | biological_process | citrate metabolic process |
| C | 0016740 | molecular_function | transferase activity |
| C | 0036440 | molecular_function | citrate synthase activity |
| C | 0046912 | molecular_function | acyltransferase activity, acyl groups converted into alkyl on transfer |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 3 |
| Details | binding site for residue CL A 501 |
| Chain | Residue |
| A | ARG428 |
| A | HOH952 |
| A | HOH991 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | binding site for residue CL C 501 |
| Chain | Residue |
| C | ARG428 |
| C | HOH874 |
| C | HOH947 |
| C | HOH971 |
Functional Information from PROSITE/UniProt
| site_id | PS00480 |
| Number of Residues | 13 |
| Details | CITRATE_SYNTHASE Citrate synthase signature. GYGHaVl.RktDPR |
| Chain | Residue | Details |
| A | GLY344-ARG356 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| Details | ACT_SITE: |
| Chain | Residue | Details |
| A | HIS301 | |
| A | HIS347 | |
| A | ASP402 | |
| C | HIS301 | |
| C | HIS347 | |
| C | ASP402 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | MOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q29RK1 |
| Chain | Residue | Details |
| A | LYS76 | |
| C | LYS76 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:Q9CZU6 |
| Chain | Residue | Details |
| A | LYS103 | |
| A | LYS193 | |
| A | LYS450 | |
| C | LYS103 | |
| C | LYS193 | |
| C | LYS450 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q9CZU6 |
| Chain | Residue | Details |
| A | SER226 | |
| C | SER226 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 10 |
| Details | MOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q9CZU6 |
| Chain | Residue | Details |
| A | LYS375 | |
| A | LYS393 | |
| A | LYS459 | |
| C | LYS321 | |
| C | LYS327 | |
| C | LYS375 | |
| C | LYS393 | |
| C | LYS459 | |
| A | LYS321 | |
| A | LYS327 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:O75390 |
| Chain | Residue | Details |
| A | LYS382 | |
| C | LYS382 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | MOD_RES: N6,N6,N6-trimethyllysine => ECO:0000269|PubMed:7093227 |
| Chain | Residue | Details |
| A | LYS395 | |
| C | LYS395 |
