2HE8
Crystal structure of 17alpha-hydroxysteroid dehydrogenase in its apo-form
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004032 | molecular_function | aldose reductase (NADPH) activity |
A | 0004033 | molecular_function | aldo-keto reductase (NADPH) activity |
A | 0005496 | molecular_function | steroid binding |
A | 0005737 | cellular_component | cytoplasm |
A | 0005829 | cellular_component | cytosol |
A | 0006694 | biological_process | steroid biosynthetic process |
A | 0008202 | biological_process | steroid metabolic process |
A | 0016229 | molecular_function | steroid dehydrogenase activity |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0033764 | molecular_function | steroid dehydrogenase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
A | 0047023 | molecular_function | androsterone dehydrogenase activity |
A | 0047024 | molecular_function | 5alpha-androstane-3beta,17beta-diol dehydrogenase activity |
A | 0047086 | molecular_function | ketosteroid monooxygenase activity |
A | 0070401 | molecular_function | NADP+ binding |
A | 0070402 | molecular_function | NADPH binding |
A | 0072555 | molecular_function | 17-beta-ketosteroid reductase activity |
A | 0072582 | molecular_function | 17-beta-hydroxysteroid dehydrogenase (NADP+) activity |
A | 1902121 | molecular_function | lithocholic acid binding |
B | 0004032 | molecular_function | aldose reductase (NADPH) activity |
B | 0004033 | molecular_function | aldo-keto reductase (NADPH) activity |
B | 0005496 | molecular_function | steroid binding |
B | 0005737 | cellular_component | cytoplasm |
B | 0005829 | cellular_component | cytosol |
B | 0006694 | biological_process | steroid biosynthetic process |
B | 0008202 | biological_process | steroid metabolic process |
B | 0016229 | molecular_function | steroid dehydrogenase activity |
B | 0016491 | molecular_function | oxidoreductase activity |
B | 0033764 | molecular_function | steroid dehydrogenase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
B | 0047023 | molecular_function | androsterone dehydrogenase activity |
B | 0047024 | molecular_function | 5alpha-androstane-3beta,17beta-diol dehydrogenase activity |
B | 0047086 | molecular_function | ketosteroid monooxygenase activity |
B | 0070401 | molecular_function | NADP+ binding |
B | 0070402 | molecular_function | NADPH binding |
B | 0072555 | molecular_function | 17-beta-ketosteroid reductase activity |
B | 0072582 | molecular_function | 17-beta-hydroxysteroid dehydrogenase (NADP+) activity |
B | 1902121 | molecular_function | lithocholic acid binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE ACT A 501 |
Chain | Residue |
A | LEU219 |
A | ALA253 |
A | ASN269 |
A | ARG276 |
A | HOH804 |
A | HOH881 |
A | HOH892 |
site_id | AC2 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE ACT A 502 |
Chain | Residue |
A | ILE79 |
A | GLU77 |
A | ASP78 |
site_id | AC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ACT A 503 |
Chain | Residue |
A | GLY226 |
A | TRP227 |
A | HOH717 |
B | TYR55 |
B | HOH738 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ACT A 504 |
Chain | Residue |
A | LEU103 |
A | GLN107 |
A | PHE108 |
A | LYS246 |
A | HOH932 |
site_id | AC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE BME A 601 |
Chain | Residue |
A | ASP143 |
A | CYS145 |
A | MET175 |
A | GLU275 |
A | ARG276 |
A | HOH943 |
site_id | AC6 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE BME A 602 |
Chain | Residue |
A | CYS29 |
A | LYS33 |
site_id | AC7 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL A 701 |
Chain | Residue |
A | MET200 |
A | TYR259 |
A | ARG263 |
A | ASP297 |
A | HOH842 |
A | HOH929 |
site_id | AC8 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GOL A 703 |
Chain | Residue |
A | HIS6 |
A | PRO17 |
A | VAL18 |
A | LEU19 |
A | GLY45 |
A | HIS47 |
A | MET281 |
A | PHE284 |
site_id | AC9 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE BME B 603 |
Chain | Residue |
B | GLU28 |
B | CYS29 |
B | LYS33 |
site_id | BC1 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GOL B 702 |
Chain | Residue |
B | LEU219 |
B | ASN269 |
B | THR270 |
B | SER271 |
B | ARG276 |
B | GLU279 |
B | ASN280 |
B | HOH824 |
Functional Information from PROSITE/UniProt
site_id | PS00062 |
Number of Residues | 18 |
Details | ALDOKETO_REDUCTASE_2 Aldo/keto reductase family signature 2. MekckdaglTKSIGVSNF |
Chain | Residue | Details |
A | MET151-PHE168 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Proton donor |
Chain | Residue | Details |
A | TYR55 | |
B | TYR55 |
site_id | SWS_FT_FI2 |
Number of Residues | 12 |
Details | BINDING: BINDING => ECO:0000269|PubMed:17034817, ECO:0000269|PubMed:17909281, ECO:0000269|PubMed:19237748 |
Chain | Residue | Details |
A | GLY20 | |
B | GLN190 | |
B | TYR216 | |
B | THR270 | |
A | ASP50 | |
A | SER166 | |
A | GLN190 | |
A | TYR216 | |
A | THR270 | |
B | GLY20 | |
B | ASP50 | |
B | SER166 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | BINDING: |
Chain | Residue | Details |
A | LYS31 | |
A | HIS117 | |
B | LYS31 | |
B | HIS117 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | SITE: Lowers pKa of active site Tyr => ECO:0000250 |
Chain | Residue | Details |
A | LYS84 | |
B | LYS84 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1mrq |
Chain | Residue | Details |
A | LYS84 | |
A | HIS117 | |
A | ASP50 | |
A | TYR55 |
site_id | CSA2 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1mrq |
Chain | Residue | Details |
B | LYS84 | |
B | HIS117 | |
B | ASP50 | |
B | TYR55 |
site_id | CSA3 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1mrq |
Chain | Residue | Details |
A | LYS84 | |
A | TYR55 |
site_id | CSA4 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1mrq |
Chain | Residue | Details |
B | LYS84 | |
B | TYR55 |