1N5D
CRYSTAL STRUCTURE OF PORCINE TESTICULAR CARBONYL REDUCTASE/ 20BETA-HYDROXYSTEROID DEHYDROGENASE
Replaces: 1HU4Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004090 | molecular_function | carbonyl reductase (NADPH) activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006629 | biological_process | lipid metabolic process |
| A | 0006805 | biological_process | xenobiotic metabolic process |
| A | 0008106 | molecular_function | alcohol dehydrogenase (NADP+) activity |
| 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 | 0042373 | biological_process | vitamin K metabolic process |
| A | 0047020 | molecular_function | 15-hydroxyprostaglandin-D dehydrogenase (NADP+) activity |
| A | 0047021 | molecular_function | 15-hydroxyprostaglandin dehydrogenase (NADP+) activity |
| A | 0050221 | molecular_function | prostaglandin E2 9-reductase activity |
| A | 0160163 | molecular_function | S-nitrosoglutathione reductase (NADPH) activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE SO4 A 400 |
| Chain | Residue |
| A | ARG57 |
| A | PHE58 |
| site_id | AC2 |
| Number of Residues | 32 |
| Details | BINDING SITE FOR RESIDUE NDP A 300 |
| Chain | Residue |
| A | LEU61 |
| A | ASP62 |
| A | ILE63 |
| A | ILE64 |
| A | ASN89 |
| A | ALA90 |
| A | ALA91 |
| A | ILE92 |
| A | ASP97 |
| A | VAL137 |
| A | SER138 |
| A | SER139 |
| A | TYR193 |
| A | LYS197 |
| A | PRO227 |
| A | GLY228 |
| A | TRP229 |
| A | VAL230 |
| A | THR232 |
| A | MET234 |
| A | GLY11 |
| A | GLY235 |
| A | HOH401 |
| A | HOH405 |
| A | HOH411 |
| A | HOH413 |
| A | ASN13 |
| A | LYS14 |
| A | GLY15 |
| A | ILE16 |
| A | ARG37 |
| A | ARG41 |
Functional Information from PROSITE/UniProt
| site_id | PS00061 |
| Number of Residues | 29 |
| Details | ADH_SHORT Short-chain dehydrogenases/reductases family signature. NgvhrkegwsDstYGVTKIGVsVLSrIYA |
| Chain | Residue | Details |
| A | ASN180-ALA208 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU10001 |
| Chain | Residue | Details |
| A | TYR193 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:11279087 |
| Chain | Residue | Details |
| A | VAL9 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:P16152 |
| Chain | Residue | Details |
| A | ASP62 | |
| A | ASN89 | |
| A | PHE94 | |
| A | GLN105 | |
| A | SER139 | |
| A | THR192 | |
| A | TYR193 | |
| A | VAL230 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P47727 |
| Chain | Residue | Details |
| A | SER1 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | MOD_RES: N6-1-carboxyethyl lysine => ECO:0000250|UniProtKB:P16152 |
| Chain | Residue | Details |
| A | LYS238 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1db3 |
| Chain | Residue | Details |
| A | TYR193 | |
| A | SER139 | |
| A | GLU141 | |
| A | LYS197 |
| site_id | CSA2 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1db3 |
| Chain | Residue | Details |
| A | ASN113 | |
| A | TYR193 | |
| A | SER139 | |
| A | LYS197 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1db3 |
| Chain | Residue | Details |
| A | LYS197 | |
| A | TRP188 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1db3 |
| Chain | Residue | Details |
| A | TYR193 | |
| A | LYS197 |
