4OAQ
Crystal structure of the R-specific Carbonyl Reductase from Candida parapsilosis ATCC 7330
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000166 | molecular_function | nucleotide binding |
A | 0006066 | biological_process | alcohol metabolic process |
A | 0008106 | molecular_function | alcohol dehydrogenase (NADP+) activity |
A | 0008270 | molecular_function | zinc ion binding |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
A | 0046872 | molecular_function | metal ion binding |
B | 0000166 | molecular_function | nucleotide binding |
B | 0006066 | biological_process | alcohol metabolic process |
B | 0008106 | molecular_function | alcohol dehydrogenase (NADP+) activity |
B | 0008270 | molecular_function | zinc ion binding |
B | 0016491 | molecular_function | oxidoreductase activity |
B | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 35 |
Details | BINDING SITE FOR RESIDUE NDP A 401 |
Chain | Residue |
A | TYR49 |
A | GLY196 |
A | LEU197 |
A | SER216 |
A | ARG217 |
A | LYS221 |
A | CYS256 |
A | ALA257 |
A | SER258 |
A | GLY259 |
A | ILE260 |
A | SER50 |
A | ASP261 |
A | VAL281 |
A | GLY282 |
A | LEU283 |
A | SER307 |
A | LEU308 |
A | LEU309 |
A | ARG356 |
A | HOH505 |
A | HOH512 |
A | HIS53 |
A | HOH540 |
A | HOH565 |
A | HOH593 |
A | HOH599 |
A | HOH673 |
A | HOH678 |
A | TRP59 |
A | CYS167 |
A | THR171 |
A | GLY193 |
A | ILE194 |
A | GLY195 |
site_id | AC2 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE DTT A 402 |
Chain | Residue |
A | TRP59 |
A | LEU283 |
A | ZN404 |
site_id | AC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN A 403 |
Chain | Residue |
A | CYS102 |
A | CYS105 |
A | CYS108 |
A | CYS116 |
site_id | AC4 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE ZN A 404 |
Chain | Residue |
A | SER50 |
A | HIS71 |
A | DTT402 |
site_id | AC5 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE EPE B 401 |
Chain | Residue |
B | TYR49 |
B | GLY196 |
B | LEU197 |
B | ALA257 |
B | ARG356 |
B | HOH513 |
B | HOH645 |
B | HOH669 |
B | HOH736 |
site_id | AC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE GOL B 402 |
Chain | Residue |
B | ASP261 |
B | LEU263 |
B | ASN264 |
B | LEU265 |
B | SER266 |
site_id | AC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN B 403 |
Chain | Residue |
B | CYS102 |
B | CYS105 |
B | CYS108 |
B | CYS116 |
site_id | AC8 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG B 404 |
Chain | Residue |
B | ASP82 |
B | HOH547 |
B | HOH639 |
B | HOH653 |
B | HOH737 |
B | HOH739 |
Functional Information from PROSITE/UniProt
site_id | PS00059 |
Number of Residues | 15 |
Details | ADH_ZINC Zinc-containing alcohol dehydrogenases signature. GHEiIGEviavGdeV |
Chain | Residue | Details |
A | GLY70-VAL84 |
site_id | PS00065 |
Number of Residues | 28 |
Details | D_2_HYDROXYACID_DH_1 D-isomer specific 2-hydroxyacid dehydrogenases NAD-binding signature. VGIIGiGGLGhlalqfanamgan.VTaFS |
Chain | Residue | Details |
A | VAL189-SER216 |