2ZAT
Crystal structure of a mammalian reductase
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000253 | molecular_function | 3-keto sterol reductase activity |
| A | 0001523 | biological_process | retinoid metabolic process |
| A | 0004090 | molecular_function | carbonyl reductase (NADPH) activity |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0005777 | cellular_component | peroxisome |
| A | 0008202 | biological_process | steroid metabolic process |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0042180 | biological_process | cellular ketone metabolic process |
| A | 0042572 | biological_process | retinol metabolic process |
| A | 0042574 | biological_process | retinal metabolic process |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0052650 | molecular_function | all-trans-retinol dehydrogenase (NADP+) activity |
| B | 0000253 | molecular_function | 3-keto sterol reductase activity |
| B | 0001523 | biological_process | retinoid metabolic process |
| B | 0004090 | molecular_function | carbonyl reductase (NADPH) activity |
| B | 0005739 | cellular_component | mitochondrion |
| B | 0005777 | cellular_component | peroxisome |
| B | 0008202 | biological_process | steroid metabolic process |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0042180 | biological_process | cellular ketone metabolic process |
| B | 0042572 | biological_process | retinol metabolic process |
| B | 0042574 | biological_process | retinal metabolic process |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0052650 | molecular_function | all-trans-retinol dehydrogenase (NADP+) activity |
| C | 0000253 | molecular_function | 3-keto sterol reductase activity |
| C | 0001523 | biological_process | retinoid metabolic process |
| C | 0004090 | molecular_function | carbonyl reductase (NADPH) activity |
| C | 0005739 | cellular_component | mitochondrion |
| C | 0005777 | cellular_component | peroxisome |
| C | 0008202 | biological_process | steroid metabolic process |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0042180 | biological_process | cellular ketone metabolic process |
| C | 0042572 | biological_process | retinol metabolic process |
| C | 0042574 | biological_process | retinal metabolic process |
| C | 0042802 | molecular_function | identical protein binding |
| C | 0052650 | molecular_function | all-trans-retinol dehydrogenase (NADP+) activity |
| D | 0000253 | molecular_function | 3-keto sterol reductase activity |
| D | 0001523 | biological_process | retinoid metabolic process |
| D | 0004090 | molecular_function | carbonyl reductase (NADPH) activity |
| D | 0005739 | cellular_component | mitochondrion |
| D | 0005777 | cellular_component | peroxisome |
| D | 0008202 | biological_process | steroid metabolic process |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0042180 | biological_process | cellular ketone metabolic process |
| D | 0042572 | biological_process | retinol metabolic process |
| D | 0042574 | biological_process | retinal metabolic process |
| D | 0042802 | molecular_function | identical protein binding |
| D | 0052650 | molecular_function | all-trans-retinol dehydrogenase (NADP+) activity |
Functional Information from PROSITE/UniProt
| site_id | PS00061 |
| Number of Residues | 29 |
| Details | ADH_SHORT Short-chain dehydrogenases/reductases family signature. SvgayhpfpnLgpYNVSKTALlGLTkNLA |
| Chain | Residue | Details |
| A | SER151-ALA179 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU10001, ECO:0000269|PubMed:18334214 |
| Chain | Residue | Details |
| A | ALA183 | |
| B | ALA183 | |
| C | ALA183 | |
| D | ALA183 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:18334214 |
| Chain | Residue | Details |
| A | ASP37 | |
| A | ILE187 | |
| B | ASP37 | |
| B | ILE187 | |
| C | ASP37 | |
| C | ILE187 | |
| D | ASP37 | |
| D | ILE187 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:Q99714 |
| Chain | Residue | Details |
| A | ALA170 | |
| B | ALA170 | |
| C | ALA170 | |
| D | ALA170 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 8 |
| Details | SITE: Responsible for the stereoselective reduction of 3-ketosteroids into 3alpha-hydroxysteroids and benzil into S-benzoin => ECO:0000269|PubMed:19056333 |
| Chain | Residue | Details |
| A | ASN177 | |
| A | VAL180 | |
| B | ASN177 | |
| B | VAL180 | |
| C | ASN177 | |
| C | VAL180 | |
| D | ASN177 | |
| D | VAL180 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | SITE: Important for the maintenance of the quaternary structure, the catalytic activity and cold stability => ECO:0000269|PubMed:18334214, ECO:0000269|PubMed:19056333 |
| Chain | Residue | Details |
| A | LEU196 | |
| B | LEU196 | |
| C | LEU196 | |
| D | LEU196 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 8 |
| Details | MOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q99LB2 |
| Chain | Residue | Details |
| A | ASP93 | |
| A | GLU217 | |
| B | ASP93 | |
| B | GLU217 | |
| C | ASP93 | |
| C | GLU217 | |
| D | ASP93 | |
| D | GLU217 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q99LB2 |
| Chain | Residue | Details |
| A | ILE221 | |
| B | ILE221 | |
| C | ILE221 | |
| D | ILE221 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 8 |
| Details | MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:Q99LB2 |
| Chain | Residue | Details |
| A | GLU228 | |
| A | SER235 | |
| B | GLU228 | |
| B | SER235 | |
| C | GLU228 | |
| C | SER235 | |
| D | GLU228 | |
| D | SER235 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1ybv |
| Chain | Residue | Details |
| A | TYR164 | |
| A | ASN123 | |
| A | SER150 | |
| A | LYS168 |
| site_id | CSA10 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ybv |
| Chain | Residue | Details |
| B | TYR164 | |
| B | LYS168 |
| site_id | CSA11 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ybv |
| Chain | Residue | Details |
| C | TYR164 | |
| C | LYS168 |
| site_id | CSA12 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ybv |
| Chain | Residue | Details |
| D | TYR164 | |
| D | LYS168 |
| site_id | CSA2 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1ybv |
| Chain | Residue | Details |
| B | TYR164 | |
| B | ASN123 | |
| B | SER150 | |
| B | LYS168 |
| site_id | CSA3 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1ybv |
| Chain | Residue | Details |
| C | TYR164 | |
| C | ASN123 | |
| C | SER150 | |
| C | LYS168 |
| site_id | CSA4 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1ybv |
| Chain | Residue | Details |
| D | TYR164 | |
| D | ASN123 | |
| D | SER150 | |
| D | LYS168 |
| site_id | CSA5 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ybv |
| Chain | Residue | Details |
| A | LEU161 | |
| A | LYS168 |
| site_id | CSA6 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ybv |
| Chain | Residue | Details |
| B | LEU161 | |
| B | LYS168 |
| site_id | CSA7 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ybv |
| Chain | Residue | Details |
| C | LEU161 | |
| C | LYS168 |
| site_id | CSA8 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ybv |
| Chain | Residue | Details |
| D | LEU161 | |
| D | LYS168 |
| site_id | CSA9 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ybv |
| Chain | Residue | Details |
| A | TYR164 | |
| A | LYS168 |
