1XL8
Crystal structure of mouse carnitine octanoyltransferase in complex with octanoylcarnitine
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0005777 | cellular_component | peroxisome |
| A | 0006091 | biological_process | generation of precursor metabolites and energy |
| A | 0006631 | biological_process | fatty acid metabolic process |
| A | 0006635 | biological_process | fatty acid beta-oxidation |
| A | 0008458 | molecular_function | carnitine O-octanoyltransferase activity |
| A | 0009410 | biological_process | response to xenobiotic stimulus |
| A | 0009437 | biological_process | carnitine metabolic process |
| A | 0015908 | biological_process | fatty acid transport |
| A | 0015936 | biological_process | coenzyme A metabolic process |
| A | 0016746 | molecular_function | acyltransferase activity |
| A | 0043231 | cellular_component | intracellular membrane-bounded organelle |
| A | 0051791 | biological_process | medium-chain fatty acid metabolic process |
| B | 0005739 | cellular_component | mitochondrion |
| B | 0005777 | cellular_component | peroxisome |
| B | 0006091 | biological_process | generation of precursor metabolites and energy |
| B | 0006631 | biological_process | fatty acid metabolic process |
| B | 0006635 | biological_process | fatty acid beta-oxidation |
| B | 0008458 | molecular_function | carnitine O-octanoyltransferase activity |
| B | 0009410 | biological_process | response to xenobiotic stimulus |
| B | 0009437 | biological_process | carnitine metabolic process |
| B | 0015908 | biological_process | fatty acid transport |
| B | 0015936 | biological_process | coenzyme A metabolic process |
| B | 0016746 | molecular_function | acyltransferase activity |
| B | 0043231 | cellular_component | intracellular membrane-bounded organelle |
| B | 0051791 | biological_process | medium-chain fatty acid metabolic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE 152 A 613 |
| Chain | Residue |
| A | TRP85 |
| A | HIS327 |
| A | TYR439 |
| A | THR441 |
| A | THR452 |
| A | SER542 |
| A | THR543 |
| A | MSE558 |
| A | HOH616 |
| site_id | AC2 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE OCB B 613 |
| Chain | Residue |
| B | TRP85 |
| B | PHE103 |
| B | HIS327 |
| B | ALA332 |
| B | MSE335 |
| B | TYR439 |
| B | THR441 |
| B | THR452 |
| B | SER542 |
| B | THR543 |
| B | SER544 |
| B | VAL546 |
| B | GLY553 |
| B | VAL555 |
| B | MSE558 |
| B | PHE566 |
| B | HOH627 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MPD B 614 |
| Chain | Residue |
| B | HIS191 |
| B | LYS268 |
| B | GLU366 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE MPD B 615 |
| Chain | Residue |
| B | LYS33 |
| B | LEU36 |
| B | GLU52 |
| B | VAL55 |
| B | GLN56 |
| B | GLN59 |
| B | GLU366 |
| B | HOH757 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MPD B 616 |
| Chain | Residue |
| B | ARG75 |
| B | SER257 |
| B | LEU258 |
| site_id | AC6 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE MPD B 617 |
| Chain | Residue |
| B | TRP85 |
| B | GLY537 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MPD B 618 |
| Chain | Residue |
| B | GLU123 |
| B | SER126 |
| B | MSE127 |
| B | PRO215 |
| B | TRP353 |
| B | GLU357 |
Functional Information from PROSITE/UniProt
| site_id | PS00439 |
| Number of Residues | 16 |
| Details | ACYLTRANSF_C_1 Acyltransferases ChoActase / COT / CPT family signature 1. LPsLPVPaLeESLkkY |
| Chain | Residue | Details |
| A | LEU20-TYR35 |
| site_id | PS00440 |
| Number of Residues | 28 |
| Details | ACYLTRANSF_C_2 Acyltransferases ChoActase / COT / CPT family signature 2. RWgDKsYnLIsfaNGifgcccDHapyDA |
| Chain | Residue | Details |
| A | ARG305-ALA332 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton acceptor => ECO:0000269|PubMed:15492013 |
| Chain | Residue | Details |
| A | HIS327 | |
| B | HIS327 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000250 |
| Chain | Residue | Details |
| A | LYS406 | |
| A | LYS410 | |
| B | LYS406 | |
| B | LYS410 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | TYR439 | |
| A | THR441 | |
| A | THR452 | |
| B | TYR439 | |
| B | THR441 | |
| B | THR452 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | MOD_RES: N-acetylmethionine => ECO:0000250|UniProtKB:Q9UKG9 |
| Chain | Residue | Details |
| A | MET1 | |
| B | MET1 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | MOD_RES: N6-succinyllysine => ECO:0007744|PubMed:23806337 |
| Chain | Residue | Details |
| A | LYS40 | |
| A | LYS57 | |
| B | LYS40 | |
| B | LYS57 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | MOD_RES: N6-succinyllysine; alternate => ECO:0007744|PubMed:23806337 |
| Chain | Residue | Details |
| A | LYS406 | |
| B | LYS406 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1q6x |
| Chain | Residue | Details |
| A | TYR90 | |
| A | PRO106 | |
| A | SER544 | |
| A | HIS327 |
| site_id | CSA2 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1q6x |
| Chain | Residue | Details |
| B | TYR90 | |
| B | PRO106 | |
| B | SER544 | |
| B | HIS327 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1q6x |
| Chain | Residue | Details |
| A | SER544 | |
| A | HIS327 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1q6x |
| Chain | Residue | Details |
| B | SER544 | |
| B | HIS327 |
