1Y5R
The crystal structure of murine 11b-hydroxysteroid dehydrogenase complexed with corticosterone
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005783 | cellular_component | endoplasmic reticulum |
| A | 0005789 | cellular_component | endoplasmic reticulum membrane |
| A | 0008202 | biological_process | steroid metabolic process |
| A | 0016020 | cellular_component | membrane |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0030324 | biological_process | lung development |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0047022 | molecular_function | 7-beta-hydroxysteroid dehydrogenase (NADP+) activity |
| A | 0050661 | molecular_function | NADP binding |
| A | 0070524 | molecular_function | 11-beta-hydroxysteroid dehydrogenase (NADP+) activity |
| B | 0005783 | cellular_component | endoplasmic reticulum |
| B | 0005789 | cellular_component | endoplasmic reticulum membrane |
| B | 0008202 | biological_process | steroid metabolic process |
| B | 0016020 | cellular_component | membrane |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0030324 | biological_process | lung development |
| B | 0042803 | molecular_function | protein homodimerization activity |
| B | 0047022 | molecular_function | 7-beta-hydroxysteroid dehydrogenase (NADP+) activity |
| B | 0050661 | molecular_function | NADP binding |
| B | 0070524 | molecular_function | 11-beta-hydroxysteroid dehydrogenase (NADP+) activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE NDP A 1 |
| Chain | Residue |
| A | C0R11 |
| A | THR92 |
| A | MET93 |
| A | ASN119 |
| A | ILE121 |
| A | ILE168 |
| A | SER169 |
| A | SER170 |
| A | TYR183 |
| A | LYS187 |
| A | LEU215 |
| A | GLY41 |
| A | GLY216 |
| A | LEU217 |
| A | ILE218 |
| A | THR220 |
| A | THR222 |
| A | ALA223 |
| A | SER43 |
| A | LYS44 |
| A | GLY45 |
| A | ILE46 |
| A | ALA65 |
| A | ARG66 |
| A | SER67 |
| site_id | AC2 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE NDP B 2 |
| Chain | Residue |
| B | C0R12 |
| B | GLY41 |
| B | SER43 |
| B | LYS44 |
| B | GLY45 |
| B | ILE46 |
| B | ARG66 |
| B | SER67 |
| B | THR92 |
| B | MET93 |
| B | ASN119 |
| B | HIS120 |
| B | ILE121 |
| B | ILE168 |
| B | SER169 |
| B | SER170 |
| B | TYR183 |
| B | LYS187 |
| B | LEU215 |
| B | GLY216 |
| B | LEU217 |
| B | ILE218 |
| B | THR220 |
| B | THR222 |
| B | ALA223 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE C0R A 11 |
| Chain | Residue |
| A | NDP1 |
| A | ILE121 |
| A | SER170 |
| A | GLN177 |
| A | TYR183 |
| A | THR222 |
| site_id | AC4 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE C0R B 12 |
| Chain | Residue |
| B | NDP2 |
| B | ILE121 |
| B | THR124 |
| B | SER170 |
| B | GLN177 |
| B | ILE180 |
| B | TYR183 |
| B | LEU217 |
| B | ILE227 |
Functional Information from PROSITE/UniProt
| site_id | PS00061 |
| Number of Residues | 29 |
| Details | ADH_SHORT Short-chain dehydrogenases/reductases family signature. SlagkmtqpmIapYSASKFALdGFFsTIR |
| Chain | Residue | Details |
| A | SER170-ARG198 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 534 |
| Details | TOPO_DOM: Lumenal => ECO:0000255 |
| Chain | Residue | Details |
| A | GLU25-ASN292 | |
| B | GLU25-ASN292 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton acceptor |
| Chain | Residue | Details |
| A | ALA185 | |
| B | ALA185 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 10 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | SER43 | |
| B | ALA185 | |
| A | GLU94 | |
| A | ILE121 | |
| A | ALA172 | |
| A | ALA185 | |
| B | SER43 | |
| B | GLU94 | |
| B | ILE121 | |
| B | ALA172 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:P28845 |
| Chain | Residue | Details |
| A | THR220 | |
| B | THR220 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
| Chain | Residue | Details |
| A | SER164 | |
| A | SER209 | |
| B | SER164 | |
| B | SER209 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| A | LYS187 | |
| A | SER170 | |
| A | TYR183 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| B | LYS187 | |
| B | SER170 | |
| B | TYR183 |
| site_id | CSA3 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| A | LYS187 | |
| A | SER170 | |
| A | TYR183 | |
| A | ASN143 |
| site_id | CSA4 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| B | LYS187 | |
| B | SER170 | |
| B | TYR183 | |
| B | ASN143 |
| site_id | CSA5 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| A | LYS187 | |
| A | ILE180 |
| site_id | CSA6 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| B | LYS187 | |
| B | ILE180 |
| site_id | CSA7 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| A | LYS187 | |
| A | TYR183 |
| site_id | CSA8 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| B | LYS187 | |
| B | TYR183 |
