1Y5M
The crystal structure of murine 11b-hydroxysteroid dehydrogenase: an important therapeutic target for diabetes
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 | 0006629 | biological_process | lipid metabolic process |
| A | 0006704 | biological_process | glucocorticoid biosynthetic process |
| A | 0006706 | biological_process | steroid catabolic process |
| A | 0006713 | biological_process | glucocorticoid catabolic process |
| A | 0008202 | biological_process | steroid metabolic process |
| A | 0008212 | biological_process | mineralocorticoid metabolic process |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0030324 | biological_process | lung development |
| A | 0031965 | cellular_component | nuclear membrane |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0043456 | biological_process | regulation of pentose-phosphate shunt |
| A | 0045177 | cellular_component | apical part of cell |
| 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 | 0005496 | molecular_function | steroid binding |
| B | 0005783 | cellular_component | endoplasmic reticulum |
| B | 0005789 | cellular_component | endoplasmic reticulum membrane |
| B | 0006629 | biological_process | lipid metabolic process |
| B | 0006704 | biological_process | glucocorticoid biosynthetic process |
| B | 0006706 | biological_process | steroid catabolic process |
| B | 0006713 | biological_process | glucocorticoid catabolic process |
| B | 0008202 | biological_process | steroid metabolic process |
| B | 0008212 | biological_process | mineralocorticoid metabolic process |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0030324 | biological_process | lung development |
| B | 0031965 | cellular_component | nuclear membrane |
| B | 0042803 | molecular_function | protein homodimerization activity |
| B | 0043456 | biological_process | regulation of pentose-phosphate shunt |
| B | 0045177 | cellular_component | apical part of cell |
| 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 | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 B 293 |
| Chain | Residue |
| B | GLY45 |
| B | ARG48 |
| B | THR220 |
| B | GLU221 |
| B | LYS238 |
| B | HOH312 |
| B | HOH341 |
| site_id | AC2 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE SO4 B 294 |
| Chain | Residue |
| B | ARG48 |
| B | LYS73 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 A 293 |
| Chain | Residue |
| A | GLY45 |
| A | ARG48 |
| A | THR220 |
| A | GLU221 |
| A | LYS238 |
| A | HOH327 |
| site_id | AC4 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE SO4 A 294 |
| Chain | Residue |
| A | ARG48 |
| site_id | AC5 |
| Number of Residues | 32 |
| Details | BINDING SITE FOR RESIDUE NDP A 1 |
| Chain | Residue |
| A | GLY41 |
| A | ALA42 |
| A | SER43 |
| A | LYS44 |
| A | GLY45 |
| A | ILE46 |
| A | ALA65 |
| A | ARG66 |
| A | SER67 |
| A | GLY91 |
| A | THR92 |
| A | MET93 |
| A | ASN119 |
| A | ILE121 |
| A | ILE168 |
| A | SER169 |
| A | SER170 |
| A | TYR183 |
| A | LYS187 |
| A | LEU215 |
| A | GLY216 |
| A | LEU217 |
| A | ILE218 |
| A | THR220 |
| A | THR222 |
| A | ALA223 |
| A | HOH312 |
| A | HOH325 |
| A | HOH327 |
| A | HOH330 |
| A | HOH337 |
| A | HOH341 |
| site_id | AC6 |
| Number of Residues | 27 |
| Details | BINDING SITE FOR RESIDUE NDP B 2 |
| 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 | ILE168 |
| B | SER169 |
| B | SER170 |
| B | TYR183 |
| B | LYS187 |
| B | LEU215 |
| B | GLY216 |
| B | LEU217 |
| B | ILE218 |
| B | THR220 |
| B | THR222 |
| B | ALA223 |
| B | HOH341 |
| site_id | AC7 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE OCT A 301 |
| Chain | Residue |
| A | GLN177 |
| B | SER280 |
| site_id | AC8 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE OCT B 302 |
| Chain | Residue |
| B | GLN177 |
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 | 2 |
| Details | Active site: {"description":"Proton acceptor"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 68 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P28845","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| A | LYS174 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| A | LYS187 | |
| A | SER170 | |
| A | TYR183 |
| site_id | CSA3 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| B | LYS187 | |
| B | SER170 | |
| B | TYR183 |
| site_id | CSA4 |
| 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 | CSA5 |
| 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 | CSA6 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| A | LYS187 | |
| A | ILE180 |
| site_id | CSA7 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| B | LYS187 | |
| B | ILE180 |
| site_id | CSA8 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| A | LYS187 | |
| A | TYR183 |
| site_id | CSA9 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| B | LYS187 | |
| B | TYR183 |
