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 |