1XU7
Crystal Structure of the Interface Open Conformation of Tetrameric 11b-HSD1
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 |
| C | 0005496 | molecular_function | steroid binding |
| C | 0005783 | cellular_component | endoplasmic reticulum |
| C | 0005789 | cellular_component | endoplasmic reticulum membrane |
| C | 0006706 | biological_process | steroid catabolic process |
| C | 0008202 | biological_process | steroid metabolic process |
| C | 0016020 | cellular_component | membrane |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0030324 | biological_process | lung development |
| C | 0042803 | molecular_function | protein homodimerization activity |
| C | 0043231 | cellular_component | intracellular membrane-bounded organelle |
| C | 0047022 | molecular_function | 7-beta-hydroxysteroid dehydrogenase (NADP+) activity |
| C | 0050661 | molecular_function | NADP binding |
| C | 0070524 | molecular_function | 11-beta-hydroxysteroid dehydrogenase (NADP+) activity |
| C | 0102196 | molecular_function | cortisol dehydrogenase activity |
| D | 0005496 | molecular_function | steroid binding |
| D | 0005783 | cellular_component | endoplasmic reticulum |
| D | 0005789 | cellular_component | endoplasmic reticulum membrane |
| 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 | 0043231 | cellular_component | intracellular membrane-bounded organelle |
| 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 activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 36 |
| Details | BINDING SITE FOR RESIDUE NDP A 522 |
| Chain | Residue |
| A | GLY41 |
| A | MET93 |
| A | ASN119 |
| A | HIS120 |
| A | ILE121 |
| A | VAL168 |
| A | SER169 |
| A | SER170 |
| A | TYR183 |
| A | LYS187 |
| A | LEU215 |
| A | SER43 |
| A | GLY216 |
| A | LEU217 |
| A | ILE218 |
| A | THR220 |
| A | THR222 |
| A | ALA223 |
| A | CPS523 |
| A | HOH536 |
| A | HOH543 |
| A | HOH557 |
| A | LYS44 |
| A | HOH597 |
| A | HOH618 |
| A | HOH685 |
| A | HOH744 |
| A | HOH797 |
| A | HOH803 |
| A | HOH964 |
| A | GLY45 |
| A | ILE46 |
| A | ALA65 |
| A | ARG66 |
| A | SER67 |
| A | THR92 |
| site_id | AC2 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE CPS A 523 |
| Chain | Residue |
| A | ILE121 |
| A | LEU171 |
| A | TYR177 |
| A | TYR183 |
| A | LEU217 |
| A | ALA223 |
| A | VAL227 |
| A | GLN234 |
| A | SER260 |
| A | SER261 |
| A | THR264 |
| A | NDP522 |
| A | HOH546 |
| A | HOH580 |
| B | TYR280 |
| B | HOH921 |
| site_id | AC3 |
| Number of Residues | 36 |
| Details | BINDING SITE FOR RESIDUE NDP B 524 |
| Chain | Residue |
| B | GLY41 |
| 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 | ILE218 |
| B | THR220 |
| B | THR222 |
| B | ALA223 |
| B | CPS525 |
| B | HOH567 |
| B | HOH575 |
| B | HOH617 |
| B | HOH642 |
| B | HOH686 |
| B | HOH741 |
| B | HOH795 |
| B | HOH820 |
| B | HOH830 |
| B | HOH945 |
| B | HOH1000 |
| site_id | AC4 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE CPS B 525 |
| Chain | Residue |
| B | NDP524 |
| B | HOH550 |
| B | HOH823 |
| A | TYR280 |
| A | HOH861 |
| B | ILE121 |
| B | LEU171 |
| B | TYR177 |
| B | TYR183 |
| B | LEU217 |
| B | ALA223 |
| B | MET233 |
| B | GLN234 |
| B | THR264 |
| site_id | AC5 |
| Number of Residues | 34 |
| Details | BINDING SITE FOR RESIDUE NDP C 526 |
| Chain | Residue |
| C | GLY41 |
| C | SER43 |
| C | LYS44 |
| C | GLY45 |
| C | ILE46 |
| C | ALA65 |
| C | ARG66 |
| C | SER67 |
| C | THR92 |
| C | MET93 |
| C | ASN119 |
| C | HIS120 |
| C | ILE121 |
| C | VAL168 |
| C | SER169 |
| C | SER170 |
| C | TYR183 |
| C | LYS187 |
| C | LEU215 |
| C | GLY216 |
| C | LEU217 |
| C | ILE218 |
| C | THR220 |
| C | THR222 |
| C | ALA223 |
| C | CPS527 |
| C | HOH566 |
| C | HOH569 |
| C | HOH625 |
| C | HOH707 |
| C | HOH793 |
| C | HOH834 |
| C | HOH932 |
| C | HOH954 |
| site_id | AC6 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE CPS C 527 |
| Chain | Residue |
| C | ILE121 |
| C | THR124 |
| C | LEU171 |
| C | TYR177 |
| C | TYR183 |
| C | LEU217 |
| C | ALA223 |
| C | MET233 |
| C | GLN234 |
| C | THR264 |
| C | NDP526 |
| C | HOH801 |
| C | HOH872 |
| D | TYR280 |
| D | HOH897 |
| site_id | AC7 |
| Number of Residues | 33 |
| Details | BINDING SITE FOR RESIDUE NDP D 528 |
| 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 | HIS120 |
| D | ILE121 |
| D | VAL168 |
| D | SER169 |
| D | SER170 |
| D | TYR183 |
| D | LYS187 |
| D | LEU215 |
| D | GLY216 |
| D | LEU217 |
| D | ILE218 |
| D | THR220 |
| D | THR222 |
| D | ALA223 |
| D | CPS529 |
| D | HOH560 |
| D | HOH576 |
| D | HOH603 |
| D | HOH606 |
| D | HOH635 |
| D | HOH829 |
| D | HOH965 |
| site_id | AC8 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE CPS D 529 |
| Chain | Residue |
| C | TYR280 |
| C | HOH708 |
| D | ILE121 |
| D | LEU171 |
| D | TYR177 |
| D | TYR183 |
| D | LEU217 |
| D | ALA223 |
| D | MET233 |
| D | GLN234 |
| D | NDP528 |
| D | HOH584 |
| D | HOH796 |
| D | HOH884 |
| site_id | AC9 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE CPS A 1 |
| Chain | Residue |
| A | PRO271 |
| A | SER272 |
| A | ILE275 |
| A | HOH998 |
| C | LEU266 |
| C | PRO271 |
| D | SER272 |
| site_id | BC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CPS C 2 |
| Chain | Residue |
| A | LEU266 |
| B | SER272 |
| C | PRO271 |
| C | SER272 |
| C | ILE275 |
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 | |
| C | GLU25-LYS292 | |
| D | GLU25-LYS292 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | ACT_SITE: Proton acceptor |
| Chain | Residue | Details |
| A | TYR183 | |
| B | TYR183 | |
| C | TYR183 | |
| D | 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 | |
| C | GLY41 | |
| C | THR92 | |
| C | ASN119 | |
| C | TYR183 | |
| C | ILE218 | |
| D | GLY41 | |
| D | THR92 | |
| D | ASN119 | |
| D | TYR183 | |
| A | THR92 | |
| D | 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 | |
| C | SER170 | |
| D | 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 | |
| C | ASN123 | |
| C | ASN162 | |
| D | ASN123 | |
| D | 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 | |
| C | ASN207 | |
| D | 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 | 4 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| B | LYS187 | |
| B | SER170 | |
| B | TYR183 | |
| B | ASN143 |
| site_id | CSA11 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| C | LYS187 | |
| C | SER170 | |
| C | TYR183 | |
| C | ASN143 |
| site_id | CSA12 |
| 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 | CSA13 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| A | LYS187 | |
| A | VAL180 |
| site_id | CSA14 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| B | LYS187 | |
| B | VAL180 |
| site_id | CSA15 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| C | LYS187 | |
| C | VAL180 |
| site_id | CSA16 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| D | LYS187 | |
| D | VAL180 |
| site_id | CSA17 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| A | LYS187 | |
| A | TYR183 |
| site_id | CSA18 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| B | LYS187 | |
| B | TYR183 |
| site_id | CSA19 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| C | LYS187 | |
| C | TYR183 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| B | LYS174 |
| site_id | CSA20 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| D | LYS187 | |
| D | TYR183 |
| site_id | CSA3 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| C | LYS174 |
| site_id | CSA4 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| D | LYS174 |
| site_id | CSA5 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| A | LYS187 | |
| A | SER170 | |
| A | TYR183 |
| site_id | CSA6 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| B | LYS187 | |
| B | SER170 | |
| B | TYR183 |
| site_id | CSA7 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| C | LYS187 | |
| C | SER170 | |
| C | TYR183 |
| site_id | CSA8 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| D | LYS187 | |
| D | SER170 | |
| D | TYR183 |
| site_id | CSA9 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| A | LYS187 | |
| A | SER170 | |
| A | TYR183 | |
| A | ASN143 |
