2PD6
Structure of human hydroxysteroid dehydrogenase type 8, HSD17B8
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004303 | molecular_function | estradiol 17-beta-dehydrogenase [NAD(P)+] activity |
A | 0005515 | molecular_function | protein binding |
A | 0005739 | cellular_component | mitochondrion |
A | 0005740 | cellular_component | mitochondrial envelope |
A | 0005759 | cellular_component | mitochondrial matrix |
A | 0005886 | cellular_component | plasma membrane |
A | 0006629 | biological_process | lipid metabolic process |
A | 0006631 | biological_process | fatty acid metabolic process |
A | 0006633 | biological_process | fatty acid biosynthetic process |
A | 0006694 | biological_process | steroid biosynthetic process |
A | 0006703 | biological_process | estrogen biosynthetic process |
A | 0008209 | biological_process | androgen metabolic process |
A | 0008210 | biological_process | estrogen metabolic process |
A | 0016020 | cellular_component | membrane |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0047035 | molecular_function | testosterone dehydrogenase (NAD+) activity |
A | 0048038 | molecular_function | quinone binding |
A | 0051290 | biological_process | protein heterotetramerization |
A | 0070404 | molecular_function | NADH binding |
A | 0106386 | molecular_function | (3R)-3-hydroxyacyl-CoA dehydrogenase (NAD+) activity |
A | 1990204 | cellular_component | oxidoreductase complex |
B | 0004303 | molecular_function | estradiol 17-beta-dehydrogenase [NAD(P)+] activity |
B | 0005515 | molecular_function | protein binding |
B | 0005739 | cellular_component | mitochondrion |
B | 0005740 | cellular_component | mitochondrial envelope |
B | 0005759 | cellular_component | mitochondrial matrix |
B | 0005886 | cellular_component | plasma membrane |
B | 0006629 | biological_process | lipid metabolic process |
B | 0006631 | biological_process | fatty acid metabolic process |
B | 0006633 | biological_process | fatty acid biosynthetic process |
B | 0006694 | biological_process | steroid biosynthetic process |
B | 0006703 | biological_process | estrogen biosynthetic process |
B | 0008209 | biological_process | androgen metabolic process |
B | 0008210 | biological_process | estrogen metabolic process |
B | 0016020 | cellular_component | membrane |
B | 0016491 | molecular_function | oxidoreductase activity |
B | 0047035 | molecular_function | testosterone dehydrogenase (NAD+) activity |
B | 0048038 | molecular_function | quinone binding |
B | 0051290 | biological_process | protein heterotetramerization |
B | 0070404 | molecular_function | NADH binding |
B | 0106386 | molecular_function | (3R)-3-hydroxyacyl-CoA dehydrogenase (NAD+) activity |
B | 1990204 | cellular_component | oxidoreductase complex |
C | 0004303 | molecular_function | estradiol 17-beta-dehydrogenase [NAD(P)+] activity |
C | 0005515 | molecular_function | protein binding |
C | 0005739 | cellular_component | mitochondrion |
C | 0005740 | cellular_component | mitochondrial envelope |
C | 0005759 | cellular_component | mitochondrial matrix |
C | 0005886 | cellular_component | plasma membrane |
C | 0006629 | biological_process | lipid metabolic process |
C | 0006631 | biological_process | fatty acid metabolic process |
C | 0006633 | biological_process | fatty acid biosynthetic process |
C | 0006694 | biological_process | steroid biosynthetic process |
C | 0006703 | biological_process | estrogen biosynthetic process |
C | 0008209 | biological_process | androgen metabolic process |
C | 0008210 | biological_process | estrogen metabolic process |
C | 0016020 | cellular_component | membrane |
C | 0016491 | molecular_function | oxidoreductase activity |
C | 0047035 | molecular_function | testosterone dehydrogenase (NAD+) activity |
C | 0048038 | molecular_function | quinone binding |
C | 0051290 | biological_process | protein heterotetramerization |
C | 0070404 | molecular_function | NADH binding |
C | 0106386 | molecular_function | (3R)-3-hydroxyacyl-CoA dehydrogenase (NAD+) activity |
C | 1990204 | cellular_component | oxidoreductase complex |
D | 0004303 | molecular_function | estradiol 17-beta-dehydrogenase [NAD(P)+] activity |
D | 0005515 | molecular_function | protein binding |
D | 0005739 | cellular_component | mitochondrion |
D | 0005740 | cellular_component | mitochondrial envelope |
D | 0005759 | cellular_component | mitochondrial matrix |
D | 0005886 | cellular_component | plasma membrane |
D | 0006629 | biological_process | lipid metabolic process |
D | 0006631 | biological_process | fatty acid metabolic process |
D | 0006633 | biological_process | fatty acid biosynthetic process |
D | 0006694 | biological_process | steroid biosynthetic process |
D | 0006703 | biological_process | estrogen biosynthetic process |
D | 0008209 | biological_process | androgen metabolic process |
D | 0008210 | biological_process | estrogen metabolic process |
D | 0016020 | cellular_component | membrane |
D | 0016491 | molecular_function | oxidoreductase activity |
D | 0047035 | molecular_function | testosterone dehydrogenase (NAD+) activity |
D | 0048038 | molecular_function | quinone binding |
D | 0051290 | biological_process | protein heterotetramerization |
D | 0070404 | molecular_function | NADH binding |
D | 0106386 | molecular_function | (3R)-3-hydroxyacyl-CoA dehydrogenase (NAD+) activity |
D | 1990204 | cellular_component | oxidoreductase complex |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 26 |
Details | BINDING SITE FOR RESIDUE NAD A 1 |
Chain | Residue |
A | GLY18 |
A | CYS103 |
A | ALA104 |
A | VAL126 |
A | ILE154 |
A | SER155 |
A | SER156 |
A | TYR169 |
A | LYS173 |
A | PRO199 |
A | GLY200 |
A | SER21 |
A | ILE202 |
A | THR204 |
A | PRO205 |
A | MET206 |
A | HOH278 |
A | HOH285 |
A | HOH337 |
A | GLY22 |
A | ILE23 |
A | ASP42 |
A | LEU43 |
A | ALA74 |
A | ASP75 |
A | VAL76 |
site_id | AC2 |
Number of Residues | 24 |
Details | BINDING SITE FOR RESIDUE NAD B 2 |
Chain | Residue |
B | GLY18 |
B | SER21 |
B | GLY22 |
B | ILE23 |
B | ASP42 |
B | LEU43 |
B | ALA74 |
B | ASP75 |
B | VAL76 |
B | CYS103 |
B | ALA104 |
B | GLY105 |
B | ILE154 |
B | SER155 |
B | SER156 |
B | TYR169 |
B | LYS173 |
B | PRO199 |
B | GLY200 |
B | ILE202 |
B | THR204 |
B | PRO205 |
B | MET206 |
B | THR207 |
site_id | AC3 |
Number of Residues | 23 |
Details | BINDING SITE FOR RESIDUE NAD C 3 |
Chain | Residue |
C | GLY18 |
C | SER21 |
C | GLY22 |
C | ILE23 |
C | ASP42 |
C | LEU43 |
C | ALA74 |
C | ASP75 |
C | VAL76 |
C | CYS103 |
C | ILE154 |
C | SER155 |
C | TYR169 |
C | LYS173 |
C | PRO199 |
C | GLY200 |
C | ILE202 |
C | THR204 |
C | PRO205 |
C | MET206 |
C | THR207 |
C | HOH288 |
C | HOH306 |
site_id | AC4 |
Number of Residues | 26 |
Details | BINDING SITE FOR RESIDUE NAD D 4 |
Chain | Residue |
D | GLY18 |
D | SER21 |
D | GLY22 |
D | ILE23 |
D | ASP42 |
D | LEU43 |
D | ALA74 |
D | ASP75 |
D | VAL76 |
D | CYS103 |
D | ALA104 |
D | GLY105 |
D | ILE154 |
D | SER155 |
D | SER156 |
D | TYR169 |
D | LYS173 |
D | PRO199 |
D | GLY200 |
D | ILE202 |
D | THR204 |
D | PRO205 |
D | MET206 |
D | THR207 |
D | HOH282 |
D | HOH291 |
Functional Information from PROSITE/UniProt
site_id | PS00061 |
Number of Residues | 29 |
Details | ADH_SHORT Short-chain dehydrogenases/reductases family signature. SivgkvgnvgQtnYAASKAGViGLTqTAA |
Chain | Residue | Details |
A | SER156-ALA184 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU10001 |
Chain | Residue | Details |
A | TYR169 | |
B | TYR169 | |
C | TYR169 | |
D | TYR169 |
site_id | SWS_FT_FI2 |
Number of Residues | 16 |
Details | BINDING: BINDING => ECO:0000269|PubMed:25203508, ECO:0000269|Ref.12, ECO:0007744|PDB:2PD6, ECO:0007744|PDB:4CQL |
Chain | Residue | Details |
A | LEU15 | |
C | ASP42 | |
C | ALA74 | |
C | TYR169 | |
D | LEU15 | |
D | ASP42 | |
D | ALA74 | |
D | TYR169 | |
A | ASP42 | |
A | ALA74 | |
A | TYR169 | |
B | LEU15 | |
B | ASP42 | |
B | ALA74 | |
B | TYR169 | |
C | LEU15 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000250 |
Chain | Residue | Details |
A | SER156 | |
B | SER156 | |
C | SER156 | |
D | SER156 |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000269|Ref.12, ECO:0007744|PDB:2PD6, ECO:0007744|PDB:4CQM |
Chain | Residue | Details |
A | ILE202 | |
B | ILE202 | |
C | ILE202 | |
D | ILE202 |
site_id | SWS_FT_FI5 |
Number of Residues | 4 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P50171 |
Chain | Residue | Details |
A | SER60 | |
B | SER60 | |
C | SER60 | |
D | SER60 |
site_id | SWS_FT_FI6 |
Number of Residues | 8 |
Details | MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P50171 |
Chain | Residue | Details |
A | LYS160 | |
A | LYS173 | |
B | LYS160 | |
B | LYS173 | |
C | LYS160 | |
C | LYS173 | |
D | LYS160 | |
D | LYS173 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1ybv |
Chain | Residue | Details |
A | SER156 | |
A | TYR169 | |
A | ASN127 | |
A | LYS173 |
site_id | CSA10 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1ybv |
Chain | Residue | Details |
B | TYR169 | |
B | LYS173 |
site_id | CSA11 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1ybv |
Chain | Residue | Details |
C | TYR169 | |
C | LYS173 |
site_id | CSA12 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1ybv |
Chain | Residue | Details |
D | TYR169 | |
D | LYS173 |
site_id | CSA2 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1ybv |
Chain | Residue | Details |
B | SER156 | |
B | TYR169 | |
B | ASN127 | |
B | LYS173 |
site_id | CSA3 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1ybv |
Chain | Residue | Details |
C | SER156 | |
C | TYR169 | |
C | ASN127 | |
C | LYS173 |
site_id | CSA4 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1ybv |
Chain | Residue | Details |
D | SER156 | |
D | TYR169 | |
D | ASN127 | |
D | LYS173 |
site_id | CSA5 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1ybv |
Chain | Residue | Details |
A | GLN166 | |
A | LYS173 |
site_id | CSA6 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1ybv |
Chain | Residue | Details |
B | GLN166 | |
B | LYS173 |
site_id | CSA7 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1ybv |
Chain | Residue | Details |
C | GLN166 | |
C | LYS173 |
site_id | CSA8 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1ybv |
Chain | Residue | Details |
D | GLN166 | |
D | LYS173 |
site_id | CSA9 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1ybv |
Chain | Residue | Details |
A | TYR169 | |
A | LYS173 |