1XA4
Crystal structure of CaiB, a type III CoA transferase in carnitine metabolism
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0008410 | molecular_function | CoA-transferase activity |
| A | 0008735 | molecular_function | L-carnitine CoA-transferase activity |
| A | 0009437 | biological_process | carnitine metabolic process |
| A | 0016740 | molecular_function | transferase activity |
| A | 0016782 | molecular_function | transferase activity, transferring sulphur-containing groups |
| A | 0042413 | biological_process | carnitine catabolic process |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0008410 | molecular_function | CoA-transferase activity |
| B | 0008735 | molecular_function | L-carnitine CoA-transferase activity |
| B | 0009437 | biological_process | carnitine metabolic process |
| B | 0016740 | molecular_function | transferase activity |
| B | 0016782 | molecular_function | transferase activity, transferring sulphur-containing groups |
| B | 0042413 | biological_process | carnitine catabolic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 A 1501 |
| Chain | Residue |
| A | SER96 |
| A | LYS97 |
| A | ARG104 |
| A | HOH1673 |
| A | HOH1683 |
| A | HOH1717 |
| site_id | AC2 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE COA B 701 |
| Chain | Residue |
| B | ASN45 |
| B | LEU71 |
| B | ASN72 |
| B | ILE73 |
| B | PHE74 |
| B | ALA95 |
| B | SER96 |
| B | LYS97 |
| B | ARG104 |
| B | LEU123 |
| B | ALA139 |
| B | TYR140 |
| B | ASP169 |
| B | GLU276 |
| B | HOH727 |
| B | HOH769 |
| B | HOH798 |
| B | HOH828 |
| B | HOH838 |
| B | HOH887 |
| B | HOH922 |
| B | GLU23 |
| B | ILE24 |
| B | ALA25 |
| site_id | AC3 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE BTB A 601 |
| Chain | Residue |
| A | TYR210 |
| A | ASP230 |
| A | TYR233 |
| A | GLU249 |
| A | VAL251 |
| A | HOH1529 |
| A | HOH1589 |
| A | HOH1721 |
| B | GLU23 |
| B | TYR140 |
| B | TYR166 |
| B | ASP169 |
| site_id | AC4 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE BTB B 602 |
| Chain | Residue |
| A | GLU23 |
| A | TYR140 |
| A | TYR166 |
| B | TYR210 |
| B | ASP230 |
| B | TYR233 |
| B | GLU249 |
| B | VAL251 |
| B | HOH710 |
| B | HOH745 |
| B | HOH767 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Nucleophile => ECO:0000255|HAMAP-Rule:MF_01050, ECO:0000305|PubMed:15518548 |
| Chain | Residue | Details |
| A | ASP169 | |
| B | ASP169 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01050, ECO:0000269|PubMed:15518548 |
| Chain | Residue | Details |
| A | LYS97 | |
| A | ARG104 | |
| B | LYS97 | |
| B | ARG104 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1xvt |
| Chain | Residue | Details |
| A | ASP169 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1xvt |
| Chain | Residue | Details |
| B | ASP169 |
| site_id | MCSA1 |
| Number of Residues | 1 |
| Details | M-CSA 531 |
| Chain | Residue | Details |
| A | ASP169 | covalently attached, electrofuge, electrophile, nucleofuge, nucleophile |
| site_id | MCSA2 |
| Number of Residues | 1 |
| Details | M-CSA 531 |
| Chain | Residue | Details |
| B | ASP169 | covalently attached, electrofuge, electrophile, nucleofuge, nucleophile |
