3CH6
Crystal Structure of 11beta-HSD1 Double Mutant (L262R, F278E) Complexed with (3,3-dimethylpiperidin-1-yl)(6-(3-fluoro-4-methylphenyl)pyridin-2-yl)methanone
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 | 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 | 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 (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 | 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 | 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 (NADP+) activity |
| D | 0005496 | molecular_function | steroid binding |
| D | 0005783 | cellular_component | endoplasmic reticulum |
| D | 0005789 | cellular_component | endoplasmic reticulum membrane |
| D | 0006629 | biological_process | lipid metabolic process |
| D | 0006706 | biological_process | steroid catabolic process |
| D | 0008202 | biological_process | steroid metabolic process |
| D | 0016020 | cellular_component | membrane |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0030324 | biological_process | lung development |
| D | 0042803 | molecular_function | protein homodimerization activity |
| D | 0047022 | molecular_function | 7-beta-hydroxysteroid dehydrogenase (NADP+) activity |
| D | 0050661 | molecular_function | NADP binding |
| D | 0070524 | molecular_function | 11-beta-hydroxysteroid dehydrogenase (NADP+) activity |
| D | 0102196 | molecular_function | cortisol dehydrogenase (NADP+) activity |
| E | 0005496 | molecular_function | steroid binding |
| E | 0005783 | cellular_component | endoplasmic reticulum |
| E | 0005789 | cellular_component | endoplasmic reticulum membrane |
| E | 0006629 | biological_process | lipid metabolic process |
| E | 0006706 | biological_process | steroid catabolic process |
| E | 0008202 | biological_process | steroid metabolic process |
| E | 0016020 | cellular_component | membrane |
| E | 0016491 | molecular_function | oxidoreductase activity |
| E | 0030324 | biological_process | lung development |
| E | 0042803 | molecular_function | protein homodimerization activity |
| E | 0047022 | molecular_function | 7-beta-hydroxysteroid dehydrogenase (NADP+) activity |
| E | 0050661 | molecular_function | NADP binding |
| E | 0070524 | molecular_function | 11-beta-hydroxysteroid dehydrogenase (NADP+) activity |
| E | 0102196 | molecular_function | cortisol dehydrogenase (NADP+) activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE NAP A 501 |
| Chain | Residue |
| A | GLY41 |
| A | MET93 |
| A | ASN119 |
| A | ILE121 |
| A | SER169 |
| A | SER170 |
| A | TYR183 |
| A | LYS187 |
| A | LEU215 |
| A | GLY216 |
| A | LEU217 |
| A | SER43 |
| A | ILE218 |
| A | THR220 |
| A | THR222 |
| A | ALA223 |
| A | LYS44 |
| A | GLY45 |
| A | ILE46 |
| A | ALA65 |
| A | ARG66 |
| A | SER67 |
| A | THR92 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE 311 A 601 |
| Chain | Residue |
| A | SER170 |
| A | TYR177 |
| A | PRO178 |
| A | MET179 |
| A | TYR183 |
| A | LEU215 |
| A | GLY216 |
| A | LEU217 |
| site_id | AC3 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE NAP B 502 |
| 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 | SER169 |
| B | SER170 |
| B | TYR183 |
| B | LYS187 |
| B | LEU215 |
| B | GLY216 |
| B | LEU217 |
| B | ILE218 |
| B | THR220 |
| B | THR222 |
| B | ALA223 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE 311 B 602 |
| Chain | Residue |
| A | TYR284 |
| B | SER170 |
| B | TYR177 |
| B | PRO178 |
| B | MET179 |
| B | TYR183 |
| B | GLY216 |
| B | LEU217 |
| site_id | AC5 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE NAP D 503 |
| Chain | Residue |
| D | GLY41 |
| D | SER43 |
| D | LYS44 |
| D | GLY45 |
| D | ILE46 |
| D | ALA65 |
| D | ARG66 |
| D | SER67 |
| D | THR92 |
| D | MET93 |
| D | ASN119 |
| D | ILE121 |
| D | SER169 |
| D | SER170 |
| D | TYR183 |
| D | LYS187 |
| D | LEU215 |
| D | GLY216 |
| D | LEU217 |
| D | ILE218 |
| D | THR220 |
| D | THR222 |
| D | ALA223 |
| site_id | AC6 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE 311 D 603 |
| Chain | Residue |
| D | LEU126 |
| D | SER170 |
| D | TYR177 |
| D | PRO178 |
| D | MET179 |
| D | TYR183 |
| D | GLY216 |
| D | LEU217 |
| E | TYR284 |
| site_id | AC7 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE NAP E 504 |
| Chain | Residue |
| E | GLY45 |
| E | ILE46 |
| E | ALA65 |
| E | ARG66 |
| E | SER67 |
| E | THR92 |
| E | MET93 |
| E | ASN119 |
| E | ILE121 |
| E | SER169 |
| E | SER170 |
| E | TYR183 |
| E | LYS187 |
| E | LEU215 |
| E | GLY216 |
| E | LEU217 |
| E | ILE218 |
| E | THR220 |
| E | THR222 |
| E | ALA223 |
| E | GLY41 |
| E | SER43 |
| E | LYS44 |
| site_id | AC8 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE 311 E 604 |
| Chain | Residue |
| D | TYR284 |
| E | SER170 |
| E | TYR177 |
| E | PRO178 |
| E | MET179 |
| E | TYR183 |
| E | GLY216 |
| E | LEU217 |
Functional Information from PROSITE/UniProt
| site_id | PS00061 |
| Number of Residues | 29 |
| Details | ADH_SHORT Short-chain dehydrogenases/reductases family signature. SlagkvaypmVaaYSASKFALdGFFsSIR |
| Chain | Residue | Details |
| A | SER170-ARG198 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1068 |
| Details | TOPO_DOM: Lumenal => ECO:0000255 |
| Chain | Residue | Details |
| A | GLU25-LYS292 | |
| B | GLU25-LYS292 | |
| D | GLU25-LYS292 | |
| E | GLU25-LYS292 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | ACT_SITE: Proton acceptor |
| Chain | Residue | Details |
| A | TYR183 | |
| B | TYR183 | |
| D | TYR183 | |
| E | TYR183 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 20 |
| 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 | |
| D | GLY41 | |
| D | THR92 | |
| D | ASN119 | |
| D | TYR183 | |
| D | ILE218 | |
| E | GLY41 | |
| E | THR92 | |
| E | ASN119 | |
| E | TYR183 | |
| A | THR92 | |
| E | ILE218 | |
| A | ASN119 | |
| A | TYR183 | |
| A | ILE218 | |
| B | GLY41 | |
| B | THR92 | |
| B | ASN119 | |
| B | TYR183 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:15513927, ECO:0007744|PDB:1XU7, ECO:0007744|PDB:1XU9 |
| Chain | Residue | Details |
| A | SER170 | |
| B | SER170 | |
| D | SER170 | |
| E | SER170 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 8 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218 |
| Chain | Residue | Details |
| A | ASN123 | |
| A | ASN162 | |
| B | ASN123 | |
| B | ASN162 | |
| D | ASN123 | |
| D | ASN162 | |
| E | ASN123 | |
| E | ASN162 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
| Chain | Residue | Details |
| A | ASN207 | |
| B | ASN207 | |
| D | ASN207 | |
| E | ASN207 |
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 | CSA10 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| A | LYS187 | |
| A | VAL180 |
| site_id | CSA11 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| B | LYS187 | |
| B | VAL180 |
| site_id | CSA12 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| D | LYS187 | |
| D | VAL180 |
| site_id | CSA13 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| E | LYS187 | |
| E | VAL180 |
| site_id | CSA14 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| A | LYS187 | |
| A | TYR183 |
| site_id | CSA15 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| B | LYS187 | |
| B | TYR183 |
| site_id | CSA16 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| D | LYS187 | |
| D | TYR183 |
| site_id | CSA17 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| E | LYS187 | |
| E | TYR183 |
| 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 | 3 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| D | LYS187 | |
| D | SER170 | |
| D | TYR183 |
| site_id | CSA5 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| E | LYS187 | |
| E | SER170 | |
| E | TYR183 |
| site_id | CSA6 |
| 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 | CSA7 |
| 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 | CSA8 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| D | LYS187 | |
| D | SER170 | |
| D | TYR183 | |
| D | ASN143 |
| site_id | CSA9 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| E | LYS187 | |
| E | SER170 | |
| E | TYR183 | |
| E | ASN143 |
