3GKB
Crystal structure of a putative enoyl-CoA hydratase from Streptomyces avermitilis
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004300 | molecular_function | enoyl-CoA hydratase activity |
A | 0006635 | biological_process | fatty acid beta-oxidation |
B | 0004300 | molecular_function | enoyl-CoA hydratase activity |
B | 0006635 | biological_process | fatty acid beta-oxidation |
C | 0004300 | molecular_function | enoyl-CoA hydratase activity |
C | 0006635 | biological_process | fatty acid beta-oxidation |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE GOL A 286 |
Chain | Residue |
A | ARG101 |
A | HOH546 |
B | ASN164 |
A | ALA124 |
A | ALA125 |
A | ALA126 |
A | TYR156 |
A | ARG160 |
A | ASP225 |
A | HOH299 |
A | HOH389 |
site_id | AC2 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE GOL B 286 |
Chain | Residue |
B | ARG101 |
B | ALA124 |
B | ALA125 |
B | ALA126 |
B | TYR156 |
B | ARG160 |
B | LEU227 |
B | HOH356 |
B | HOH378 |
C | ASN164 |
site_id | AC3 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE GOL C 286 |
Chain | Residue |
A | ASN164 |
C | ARG101 |
C | ALA124 |
C | ALA125 |
C | ALA126 |
C | ARG160 |
C | ASP225 |
C | HOH318 |
C | HOH352 |
C | HOH355 |