3G49
N-(Pyridin-2-yl) Arylsulfonamide Inhibitors of 11b-Hydroxysteroid Dehydrogenase Type 1: Discovery of PF-915275
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 | 27 |
| Details | BINDING SITE FOR RESIDUE NAP A 2002 |
| Chain | Residue |
| A | GLY16 |
| A | MET68 |
| A | ASN94 |
| A | HIS95 |
| A | VAL96 |
| A | VAL143 |
| A | SER144 |
| A | SER145 |
| A | TYR158 |
| A | LYS162 |
| A | LEU190 |
| A | SER18 |
| A | GLY191 |
| A | LEU192 |
| A | ILE193 |
| A | THR195 |
| A | THR197 |
| A | ALA198 |
| A | 3G42004 |
| A | HOH2238 |
| A | LYS19 |
| A | GLY20 |
| A | ILE21 |
| A | ALA40 |
| A | ARG41 |
| A | SER42 |
| A | SER67 |
| site_id | AC2 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE 3G4 A 2004 |
| Chain | Residue |
| A | ASN99 |
| A | SER145 |
| A | VAL146 |
| A | ALA147 |
| A | ILE155 |
| A | TYR158 |
| A | LEU190 |
| A | GLY191 |
| A | LEU192 |
| A | TYR206 |
| A | NAP2002 |
| site_id | AC3 |
| Number of Residues | 30 |
| Details | BINDING SITE FOR RESIDUE NAP B 2003 |
| Chain | Residue |
| B | GLY279 |
| B | SER281 |
| B | GLY283 |
| B | ILE284 |
| B | ALA303 |
| B | ARG304 |
| B | SER305 |
| B | GLY329 |
| B | SER330 |
| B | MET331 |
| B | ASN357 |
| B | HIS358 |
| B | VAL359 |
| B | TYR361 |
| B | VAL406 |
| B | SER407 |
| B | SER408 |
| B | TYR421 |
| B | LYS425 |
| B | LEU453 |
| B | GLY454 |
| B | LEU455 |
| B | ILE456 |
| B | THR458 |
| B | THR460 |
| B | ALA461 |
| B | HOH2060 |
| B | HOH2080 |
| B | HOH2100 |
| B | HOH2304 |
| site_id | AC4 |
| Number of Residues | 27 |
| Details | BINDING SITE FOR RESIDUE NAP C 2000 |
| Chain | Residue |
| C | GLY542 |
| C | SER544 |
| C | LYS545 |
| C | GLY546 |
| C | ILE547 |
| C | ALA566 |
| C | ARG567 |
| C | SER568 |
| C | SER593 |
| C | MET594 |
| C | ASN620 |
| C | HIS621 |
| C | VAL622 |
| C | VAL669 |
| C | SER670 |
| C | SER671 |
| C | TYR684 |
| C | LYS688 |
| C | LEU716 |
| C | GLY717 |
| C | LEU718 |
| C | ILE719 |
| C | THR721 |
| C | THR723 |
| C | ALA724 |
| C | HOH2093 |
| C | HOH2169 |
| site_id | AC5 |
| Number of Residues | 28 |
| Details | BINDING SITE FOR RESIDUE NAP D 2001 |
| Chain | Residue |
| D | ILE810 |
| D | ARG830 |
| D | SER831 |
| D | GLY855 |
| D | SER856 |
| D | MET857 |
| D | ASN883 |
| D | HIS884 |
| D | VAL885 |
| D | VAL932 |
| D | SER933 |
| D | SER934 |
| D | TYR947 |
| D | LYS951 |
| D | LEU979 |
| D | GLY980 |
| D | LEU981 |
| D | ILE982 |
| D | THR984 |
| D | THR986 |
| D | ALA987 |
| D | 3G42007 |
| D | HOH2141 |
| D | HOH2351 |
| D | GLY805 |
| D | SER807 |
| D | LYS808 |
| D | GLY809 |
| site_id | AC6 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE 3G4 D 2007 |
| Chain | Residue |
| D | VAL885 |
| D | ASN888 |
| D | SER934 |
| D | VAL935 |
| D | ALA936 |
| D | TYR941 |
| D | ILE944 |
| D | TYR947 |
| D | LEU979 |
| D | GLY980 |
| D | LEU981 |
| D | TYR995 |
| D | NAP2001 |
Functional Information from PROSITE/UniProt
| site_id | PS00061 |
| Number of Residues | 29 |
| Details | ADH_SHORT Short-chain dehydrogenases/reductases family signature. SvagkityplIapYSASKFALdGFFsTLR |
| Chain | Residue | Details |
| A | SER145-ARG173 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1100 |
| Details | TOPO_DOM: Lumenal => ECO:0000255 |
| Chain | Residue | Details |
| A | GLU0-ALA275 | |
| B | GLU263-ALA538 | |
| C | GLU526-ALA801 | |
| D | GLU789-ALA1064 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU10001 |
| Chain | Residue | Details |
| A | TYR158 | |
| B | TYR421 | |
| C | TYR684 | |
| D | TYR947 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 20 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:15542590, ECO:0000269|PubMed:19473839, ECO:0000269|PubMed:19507261 |
| Chain | Residue | Details |
| A | GLY16 | |
| B | ILE456 | |
| C | GLY542 | |
| C | SER593 | |
| C | ASN620 | |
| C | TYR684 | |
| C | ILE719 | |
| D | GLY805 | |
| D | SER856 | |
| D | ASN883 | |
| D | TYR947 | |
| A | SER67 | |
| D | ILE982 | |
| A | ASN94 | |
| A | TYR158 | |
| A | ILE193 | |
| B | GLY279 | |
| B | SER330 | |
| B | ASN357 | |
| B | TYR421 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000250 |
| Chain | Residue | Details |
| A | SER145 | |
| B | SER408 | |
| C | SER671 | |
| D | SER934 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
| Chain | Residue | Details |
| A | ASN182 | |
| B | ASN445 | |
| C | ASN708 | |
| D | ASN971 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| A | SER145 | |
| A | TYR158 | |
| A | LYS162 |
| site_id | CSA10 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| B | LYS425 | |
| B | ILE418 |
| site_id | CSA11 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| C | ILE681 | |
| C | LYS688 |
| site_id | CSA12 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| D | LYS951 | |
| D | ILE944 |
| site_id | CSA13 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| A | TYR158 | |
| A | LYS162 |
| site_id | CSA14 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| B | TYR421 | |
| B | LYS425 |
| site_id | CSA15 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| C | TYR684 | |
| C | LYS688 |
| site_id | CSA16 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| D | LYS951 | |
| D | TYR947 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| B | SER408 | |
| B | TYR421 | |
| B | LYS425 |
| site_id | CSA3 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| C | SER671 | |
| C | TYR684 | |
| C | LYS688 |
| site_id | CSA4 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| D | LYS951 | |
| D | SER934 | |
| D | TYR947 |
| site_id | CSA5 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| A | ASN118 | |
| A | SER145 | |
| A | TYR158 | |
| A | LYS162 |
| site_id | CSA6 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| B | TYR421 | |
| B | SER408 | |
| B | ASN381 | |
| B | LYS425 |
| site_id | CSA7 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| C | ASN644 | |
| C | SER671 | |
| C | TYR684 | |
| C | LYS688 |
| site_id | CSA8 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| D | LYS951 | |
| D | TYR947 | |
| D | ASN907 | |
| D | SER934 |
| site_id | CSA9 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1eq2 |
| Chain | Residue | Details |
| A | ILE155 | |
| A | LYS162 |
