4P38
Human 11beta-Hydroxysteroid Dehydrogenase Type 1 in complex with AZD8329
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005496 | molecular_function | steroid binding |
A | 0005783 | cellular_component | endoplasmic reticulum |
A | 0005789 | cellular_component | endoplasmic reticulum membrane |
A | 0006706 | biological_process | steroid catabolic process |
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 | 0043231 | cellular_component | intracellular membrane-bounded organelle |
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 |
A | 0102196 | molecular_function | cortisol dehydrogenase activity |
B | 0005496 | molecular_function | steroid binding |
B | 0005783 | cellular_component | endoplasmic reticulum |
B | 0005789 | cellular_component | endoplasmic reticulum membrane |
B | 0006706 | biological_process | steroid catabolic process |
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 | 0043231 | cellular_component | intracellular membrane-bounded organelle |
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 |
B | 0102196 | molecular_function | cortisol dehydrogenase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 26 |
Details | binding site for residue NDP A 301 |
Chain | Residue |
A | GLY41 |
A | THR92 |
A | MET93 |
A | ASN119 |
A | ILE121 |
A | VAL168 |
A | SER169 |
A | SER170 |
A | TYR183 |
A | LYS187 |
A | LEU215 |
A | ALA42 |
A | GLY216 |
A | LEU217 |
A | ILE218 |
A | THR220 |
A | THR222 |
A | ALA223 |
A | 21T302 |
A | SER43 |
A | LYS44 |
A | GLY45 |
A | ILE46 |
A | ALA65 |
A | ARG66 |
A | SER67 |
site_id | AC2 |
Number of Residues | 11 |
Details | binding site for residue 21T A 302 |
Chain | Residue |
A | LEU126 |
A | SER170 |
A | LEU171 |
A | TYR183 |
A | LEU215 |
A | GLY216 |
A | LEU217 |
A | ALA223 |
A | NDP301 |
B | TYR280 |
B | TYR284 |
site_id | AC3 |
Number of Residues | 4 |
Details | binding site for residue CL A 303 |
Chain | Residue |
A | GLY45 |
A | ARG48 |
A | GLU221 |
A | LYS238 |
site_id | AC4 |
Number of Residues | 30 |
Details | binding site for residue NDP B 301 |
Chain | Residue |
B | GLY41 |
B | ALA42 |
B | SER43 |
B | LYS44 |
B | GLY45 |
B | ILE46 |
B | ALA65 |
B | ARG66 |
B | SER67 |
B | THR92 |
B | MET93 |
B | ASN119 |
B | HIS120 |
B | ILE121 |
B | VAL168 |
B | SER169 |
B | SER170 |
B | TYR183 |
B | LYS187 |
B | LEU215 |
B | GLY216 |
B | LEU217 |
B | ILE218 |
B | THR220 |
B | THR222 |
B | ALA223 |
B | 21T302 |
B | HOH402 |
B | HOH405 |
B | HOH406 |
site_id | AC5 |
Number of Residues | 10 |
Details | binding site for residue 21T B 302 |
Chain | Residue |
A | TYR280 |
A | TYR284 |
B | SER170 |
B | LEU171 |
B | TYR177 |
B | TYR183 |
B | LEU215 |
B | GLY216 |
B | LEU217 |
B | NDP301 |
site_id | AC6 |
Number of Residues | 4 |
Details | binding site for residue CL B 303 |
Chain | Residue |
B | GLY45 |
B | GLU221 |
B | LYS238 |
B | HOH406 |
Functional Information from PROSITE/UniProt
site_id | PS00061 |
Number of Residues | 29 |
Details | ADH_SHORT Short-chain dehydrogenases/reductases family signature. SlagkvayplVaaYSASKFALdGFFsSIR |
Chain | Residue | Details |
A | SER170-ARG198 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Proton acceptor |
Chain | Residue | Details |
A | TYR183 | |
B | TYR183 |
site_id | SWS_FT_FI2 |
Number of Residues | 10 |
Details | BINDING: BINDING => ECO:0000269|PubMed:15513927, ECO:0000269|PubMed:17919905, ECO:0000269|PubMed:18069989, ECO:0000269|PubMed:18485702, ECO:0000269|PubMed:18553955, ECO:0000269|PubMed:19217779 |
Chain | Residue | Details |
A | GLY41 | |
B | ILE218 | |
A | THR92 | |
A | ASN119 | |
A | TYR183 | |
A | ILE218 | |
B | GLY41 | |
B | THR92 | |
B | ASN119 | |
B | TYR183 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:15513927, ECO:0007744|PDB:1XU7, ECO:0007744|PDB:1XU9 |
Chain | Residue | Details |
A | SER170 | |
B | SER170 |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218 |
Chain | Residue | Details |
A | ASN123 | |
A | ASN162 | |
B | ASN123 | |
B | ASN162 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
Chain | Residue | Details |
A | ASN207 | |
B | ASN207 |