6BOL
Crystal structure of mutant 2-methylcitrate synthase mcsAG419A from Aspergillus fumigatus.
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 | 0006099 | biological_process | tricarboxylic acid cycle |
| A | 0016740 | molecular_function | transferase activity |
| 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 | 0004108 | molecular_function | citrate (Si)-synthase activity |
| B | 0005739 | cellular_component | mitochondrion |
| B | 0005759 | cellular_component | mitochondrial matrix |
| B | 0006099 | biological_process | tricarboxylic acid cycle |
| B | 0016740 | molecular_function | transferase activity |
| 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 | 4 |
| Details | binding site for residue PO4 B 501 |
| Chain | Residue |
| A | ARG344 |
| B | GLY189 |
| B | LEU190 |
| B | SER191 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | binding site for residue OAA A 501 |
| Chain | Residue |
| A | LYS46 |
| A | LEU49 |
| A | HIS95 |
| B | LEU461 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue OAA A 502 |
| Chain | Residue |
| A | LYS192 |
| A | ALA193 |
| A | HOH660 |
| A | ARG47 |
| site_id | AC4 |
| Number of Residues | 2 |
| Details | binding site for residue PO4 A 503 |
| Chain | Residue |
| A | LYS54 |
| A | GLN421 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | binding site for residue PO4 A 504 |
| Chain | Residue |
| A | HIS269 |
| A | ASN273 |
| A | HIS305 |
| A | HIS351 |
| A | HOH606 |
| A | HOH616 |
| B | ARG454 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | binding site for residue CL A 505 |
| Chain | Residue |
| A | ASP34 |
| A | LEU35 |
| A | HOH662 |
Functional Information from PROSITE/UniProt
| site_id | PS00480 |
| Number of Residues | 13 |
| Details | CITRATE_SYNTHASE Citrate synthase signature. GYGHgVl.RkpDPR |
| Chain | Residue | Details |
| B | GLY348-ARG360 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| Details | ACT_SITE: ACT_SITE => ECO:0000250|UniProtKB:O34002 |
| Chain | Residue | Details |
| B | HIS305 | |
| B | HIS351 | |
| B | ASP408 | |
| A | HIS305 | |
| A | HIS351 | |
| A | ASP408 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:I6Y9Q3 |
| Chain | Residue | Details |
| B | HIS269 | |
| B | ARG360 | |
| B | ARG434 | |
| A | HIS269 | |
| A | ARG360 | |
| A | ARG434 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:O34002 |
| Chain | Residue | Details |
| B | VAL345 | |
| A | VAL345 |
