3O3N
(R)-2-hydroxyisocaproyl-CoA dehydratase in complex with its substrate (R)-2-hydroxyisocaproyl-CoA
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0006551 | biological_process | L-leucine metabolic process |
| A | 0016829 | molecular_function | lyase activity |
| A | 0016836 | molecular_function | hydro-lyase activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
| B | 0006551 | biological_process | L-leucine metabolic process |
| B | 0016829 | molecular_function | lyase activity |
| B | 0016836 | molecular_function | hydro-lyase activity |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
| C | 0006551 | biological_process | L-leucine metabolic process |
| C | 0016829 | molecular_function | lyase activity |
| C | 0016836 | molecular_function | hydro-lyase activity |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
| D | 0006551 | biological_process | L-leucine metabolic process |
| D | 0016829 | molecular_function | lyase activity |
| D | 0016836 | molecular_function | hydro-lyase activity |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SF4 A 409 |
| Chain | Residue |
| A | CYS84 |
| A | CYS117 |
| A | CYS346 |
| A | IRC410 |
| site_id | AC2 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE IRC A 410 |
| Chain | Residue |
| A | VAL38 |
| A | GLU55 |
| A | ASN56 |
| A | GLY60 |
| A | TYR86 |
| A | PHE215 |
| A | THR216 |
| A | MET218 |
| A | ALA219 |
| A | ILE265 |
| A | TRP268 |
| A | TYR290 |
| A | TRP294 |
| A | MET313 |
| A | SF4409 |
| A | HOH1272 |
| A | HOH1507 |
| A | ASN12 |
| A | ASP13 |
| A | LEU15 |
| A | ALA16 |
| A | SER37 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SF4 B 386 |
| Chain | Residue |
| B | CYS72 |
| B | ILE74 |
| B | MET75 |
| B | CYS99 |
| B | LEU102 |
| B | CYS325 |
| B | ASP326 |
| B | H2S387 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE H2S B 387 |
| Chain | Residue |
| B | PRO35 |
| B | VAL36 |
| B | SF4386 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SF4 C 409 |
| Chain | Residue |
| C | CYS84 |
| C | CYS117 |
| C | CYS346 |
| C | IRC410 |
| site_id | AC6 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE IRC C 410 |
| Chain | Residue |
| A | HOH704 |
| A | HOH974 |
| B | HOH1263 |
| B | HOH1373 |
| C | ASN12 |
| C | LEU15 |
| C | VAL38 |
| C | GLU55 |
| C | ASN56 |
| C | GLY60 |
| C | LYS64 |
| C | TYR86 |
| C | LEU102 |
| C | PHE215 |
| C | MET218 |
| C | ALA219 |
| C | ILE265 |
| C | TYR290 |
| C | TRP294 |
| C | MET313 |
| C | PHE314 |
| C | SF4409 |
| C | HOH868 |
| C | HOH917 |
| C | HOH1377 |
| C | HOH1527 |
| site_id | AC7 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE SF4 D 386 |
| Chain | Residue |
| D | CYS72 |
| D | ILE74 |
| D | MET75 |
| D | CYS99 |
| D | LEU102 |
| D | ILE237 |
| D | MET322 |
| D | CYS325 |
| D | PRO327 |
| D | H2S387 |
| site_id | AC8 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE H2S D 387 |
| Chain | Residue |
| D | PRO35 |
| D | SF4386 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:21366233 |
| Chain | Residue | Details |
| B | CYS72 | |
| B | CYS99 | |
| B | CYS325 | |
| D | CYS72 | |
| D | CYS99 | |
| D | CYS325 | |
| C | CYS117 | |
| C | CYS346 |
