6BOO
Crystal structure of 2-methylcitrate synthase from Aspergillus fumigatus with oxaloacetate and coenzyme-A.
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 |
C | 0004108 | molecular_function | citrate (Si)-synthase activity |
C | 0005739 | cellular_component | mitochondrion |
C | 0005759 | cellular_component | mitochondrial matrix |
C | 0006099 | biological_process | tricarboxylic acid cycle |
C | 0016740 | molecular_function | transferase activity |
C | 0019629 | biological_process | propionate catabolic process, 2-methylcitrate cycle |
C | 0036440 | molecular_function | citrate synthase activity |
C | 0042802 | molecular_function | identical protein binding |
C | 0046912 | molecular_function | acyltransferase activity, acyl groups converted into alkyl on transfer |
C | 0050440 | molecular_function | 2-methylcitrate synthase activity |
D | 0004108 | molecular_function | citrate (Si)-synthase activity |
D | 0005739 | cellular_component | mitochondrion |
D | 0005759 | cellular_component | mitochondrial matrix |
D | 0006099 | biological_process | tricarboxylic acid cycle |
D | 0016740 | molecular_function | transferase activity |
D | 0019629 | biological_process | propionate catabolic process, 2-methylcitrate cycle |
D | 0036440 | molecular_function | citrate synthase activity |
D | 0042802 | molecular_function | identical protein binding |
D | 0046912 | molecular_function | acyltransferase activity, acyl groups converted into alkyl on transfer |
D | 0050440 | molecular_function | 2-methylcitrate synthase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 13 |
Details | binding site for residue OAA B 501 |
Chain | Residue |
B | HIS269 |
B | HOH603 |
B | HOH604 |
B | HOH618 |
C | ARG454 |
B | ASN273 |
B | HIS305 |
B | HIS351 |
B | ARG360 |
B | ASP408 |
B | PHE430 |
B | ARG434 |
B | COA503 |
site_id | AC2 |
Number of Residues | 2 |
Details | binding site for residue OAA B 502 |
Chain | Residue |
A | GLU63 |
D | ASP58 |
site_id | AC3 |
Number of Residues | 22 |
Details | binding site for residue COA B 503 |
Chain | Residue |
B | ARG74 |
B | LEU304 |
B | HIS305 |
B | ALA308 |
B | LEU340 |
B | VAL345 |
B | VAL346 |
B | PRO347 |
B | GLY348 |
B | TYR349 |
B | GLY350 |
B | HIS351 |
B | GLY352 |
B | LEU394 |
B | LYS399 |
B | THR400 |
B | LYS401 |
B | ASN406 |
B | ASP408 |
B | OAA501 |
C | LYS192 |
C | HOH641 |
site_id | AC4 |
Number of Residues | 12 |
Details | binding site for residue OAA A 501 |
Chain | Residue |
A | HIS269 |
A | ASN273 |
A | HIS305 |
A | HIS351 |
A | ARG360 |
A | ASP408 |
A | PHE430 |
A | ARG434 |
A | COA502 |
A | HOH614 |
A | HOH617 |
D | ARG454 |
site_id | AC5 |
Number of Residues | 20 |
Details | binding site for residue COA A 502 |
Chain | Residue |
A | ARG74 |
A | LEU304 |
A | ALA308 |
A | LEU340 |
A | VAL345 |
A | VAL346 |
A | GLY348 |
A | TYR349 |
A | GLY350 |
A | HIS351 |
A | GLY352 |
A | LEU394 |
A | LYS399 |
A | THR400 |
A | LYS401 |
A | ASN406 |
A | ASP408 |
A | OAA501 |
A | HOH616 |
D | LYS192 |
site_id | AC6 |
Number of Residues | 2 |
Details | binding site for residue OAA C 501 |
Chain | Residue |
C | ARG74 |
C | LYS401 |
site_id | AC7 |
Number of Residues | 4 |
Details | binding site for residue OAA D 501 |
Chain | Residue |
D | ARG74 |
D | HIS351 |
D | GLY352 |
D | LYS401 |
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 | 12 |
Details | ACT_SITE: ACT_SITE => ECO:0000250|UniProtKB:O34002 |
Chain | Residue | Details |
B | HIS305 | |
D | HIS305 | |
D | HIS351 | |
D | ASP408 | |
B | HIS351 | |
B | ASP408 | |
A | HIS305 | |
A | HIS351 | |
A | ASP408 | |
C | HIS305 | |
C | HIS351 | |
C | ASP408 |
site_id | SWS_FT_FI2 |
Number of Residues | 12 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:I6Y9Q3 |
Chain | Residue | Details |
B | HIS269 | |
D | HIS269 | |
D | ARG360 | |
D | ARG434 | |
B | ARG360 | |
B | ARG434 | |
A | HIS269 | |
A | ARG360 | |
A | ARG434 | |
C | HIS269 | |
C | ARG360 | |
C | ARG434 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:O34002 |
Chain | Residue | Details |
B | VAL345 | |
A | VAL345 | |
C | VAL345 | |
D | VAL345 |