5UQR
Crystal structure of 2-methylcitrate synthase from Aspergillus fumigatus
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| 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 | 0019629 | biological_process | propionate catabolic process, 2-methylcitrate cycle |
| A | 0036440 | molecular_function | citrate synthase activity |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0046912 | molecular_function | acyltransferase activity, acyl groups converted into alkyl on transfer |
| A | 0050440 | molecular_function | 2-methylcitrate synthase activity |
| B | 0005739 | cellular_component | mitochondrion |
| B | 0005759 | cellular_component | mitochondrial matrix |
| B | 0005975 | biological_process | carbohydrate metabolic process |
| B | 0006099 | biological_process | tricarboxylic acid cycle |
| B | 0019629 | biological_process | propionate catabolic process, 2-methylcitrate cycle |
| B | 0036440 | molecular_function | citrate synthase activity |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0046912 | molecular_function | acyltransferase activity, acyl groups converted into alkyl on transfer |
| B | 0050440 | molecular_function | 2-methylcitrate synthase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 9 |
| Details | binding site for residue OAA A 501 |
| Chain | Residue |
| A | HIS269 |
| A | ASN273 |
| A | HIS305 |
| A | HIS351 |
| A | ARG360 |
| A | ARG434 |
| A | HOH939 |
| A | HOH972 |
| B | ARG454 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | binding site for residue NA A 502 |
| Chain | Residue |
| A | HOH690 |
| A | HOH954 |
| A | HOH1038 |
| A | HOH1189 |
| A | HOH1234 |
| B | NA503 |
| B | HOH1080 |
| site_id | AC3 |
| Number of Residues | 10 |
| Details | binding site for residue OAA B 501 |
| Chain | Residue |
| A | ARG454 |
| B | HIS269 |
| B | ASN273 |
| B | HIS305 |
| B | HIS351 |
| B | ARG360 |
| B | ARG434 |
| B | 8JD504 |
| B | HOH751 |
| B | HOH844 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | binding site for residue NA B 502 |
| Chain | Residue |
| A | HOH821 |
| A | HOH864 |
| B | GLY398 |
| B | NA503 |
| B | HOH736 |
| B | HOH995 |
| B | HOH1045 |
| site_id | AC5 |
| Number of Residues | 8 |
| Details | binding site for residue NA B 503 |
| Chain | Residue |
| A | NA502 |
| A | HOH1189 |
| B | GLY398 |
| B | NA502 |
| B | HOH828 |
| B | HOH1045 |
| B | HOH1047 |
| B | HOH1080 |
| site_id | AC6 |
| Number of Residues | 27 |
| Details | binding site for residue 8JD B 504 |
| Chain | Residue |
| A | LYS192 |
| B | ARG74 |
| B | LEU304 |
| B | HIS305 |
| B | ALA308 |
| B | LEU340 |
| B | VAL345 |
| B | VAL346 |
| B | GLY348 |
| B | TYR349 |
| B | GLY350 |
| B | HIS351 |
| B | GLY352 |
| B | LYS399 |
| B | THR400 |
| B | LYS401 |
| B | ASN406 |
| B | ASP408 |
| B | PHE430 |
| B | OAA501 |
| B | HOH607 |
| B | HOH629 |
| B | HOH637 |
| B | HOH710 |
| B | HOH858 |
| B | HOH864 |
| B | HOH877 |
Functional Information from PROSITE/UniProt
| site_id | PS00480 |
| Number of Residues | 13 |
| Details | CITRATE_SYNTHASE Citrate synthase signature. GYGHgVl.RkpDPR |
| Chain | Residue | Details |
| A | GLY348-ARG360 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| Details | Active site: {"evidences":[{"source":"UniProtKB","id":"O34002","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 18 |
| Details | Binding site: {"description":"in chain B","evidences":[{"source":"UniProtKB","id":"B0YD89","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 10 |
| Details | Binding site: {"description":"in chain A","evidences":[{"source":"UniProtKB","id":"B0YD89","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
