3QWF
Crystal structure of the 17beta-hydroxysteroid dehydrogenase from Cochliobolus lunatus
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016614 | molecular_function | oxidoreductase activity, acting on CH-OH group of donors |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016614 | molecular_function | oxidoreductase activity, acting on CH-OH group of donors |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0016614 | molecular_function | oxidoreductase activity, acting on CH-OH group of donors |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0016614 | molecular_function | oxidoreductase activity, acting on CH-OH group of donors |
| E | 0000166 | molecular_function | nucleotide binding |
| E | 0016491 | molecular_function | oxidoreductase activity |
| E | 0016614 | molecular_function | oxidoreductase activity, acting on CH-OH group of donors |
| F | 0000166 | molecular_function | nucleotide binding |
| F | 0016491 | molecular_function | oxidoreductase activity |
| F | 0016614 | molecular_function | oxidoreductase activity, acting on CH-OH group of donors |
| G | 0000166 | molecular_function | nucleotide binding |
| G | 0016491 | molecular_function | oxidoreductase activity |
| G | 0016614 | molecular_function | oxidoreductase activity, acting on CH-OH group of donors |
| H | 0000166 | molecular_function | nucleotide binding |
| H | 0016491 | molecular_function | oxidoreductase activity |
| H | 0016614 | molecular_function | oxidoreductase activity, acting on CH-OH group of donors |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL A 301 |
| Chain | Residue |
| A | LEU16 |
| A | LYS19 |
| A | GLY145 |
| A | GLY146 |
| A | VAL251 |
| A | SER252 |
| A | LYS253 |
| A | HOH479 |
| A | HOH522 |
| site_id | AC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL A 302 |
| Chain | Residue |
| A | ASN154 |
| A | PHE159 |
| A | GLY199 |
| A | TYR212 |
| A | ALA228 |
| A | ALA231 |
| A | HOH532 |
| A | HOH561 |
| A | HOH571 |
| site_id | AC3 |
| Number of Residues | 36 |
| Details | BINDING SITE FOR RESIDUE NAP A 303 |
| Chain | Residue |
| A | GLY25 |
| A | ARG28 |
| A | GLY29 |
| A | ILE30 |
| A | ALA50 |
| A | ASN51 |
| A | SER52 |
| A | ALA75 |
| A | ASP76 |
| A | ILE77 |
| A | ARG78 |
| A | ASN103 |
| A | SER104 |
| A | GLY105 |
| A | LEU126 |
| A | THR151 |
| A | SER152 |
| A | SER153 |
| A | TYR167 |
| A | LYS171 |
| A | PRO197 |
| A | GLY198 |
| A | GLY199 |
| A | THR200 |
| A | THR202 |
| A | ASP203 |
| A | MET204 |
| A | HOH406 |
| A | HOH418 |
| A | HOH420 |
| A | HOH424 |
| A | HOH439 |
| A | HOH449 |
| A | HOH462 |
| A | HOH497 |
| A | HOH534 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL B 301 |
| Chain | Residue |
| B | GLY14 |
| B | HIS37 |
| B | ASN245 |
| B | GLY248 |
| B | PHE249 |
| B | HOH494 |
| site_id | AC5 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL B 302 |
| Chain | Residue |
| B | LEU16 |
| B | LYS19 |
| B | GLY145 |
| B | VAL251 |
| B | SER252 |
| B | LYS253 |
| B | HOH432 |
| B | HOH434 |
| site_id | AC6 |
| Number of Residues | 34 |
| Details | BINDING SITE FOR RESIDUE NAP B 303 |
| Chain | Residue |
| B | HOH460 |
| B | HOH484 |
| B | HOH557 |
| B | GLY25 |
| B | ARG28 |
| B | GLY29 |
| B | ILE30 |
| B | ALA50 |
| B | ASN51 |
| B | SER52 |
| B | ALA75 |
| B | ASP76 |
| B | ILE77 |
| B | ARG78 |
| B | ASN103 |
| B | SER104 |
| B | GLY105 |
| B | LEU126 |
| B | THR151 |
| B | SER152 |
| B | SER153 |
| B | TYR167 |
| B | LYS171 |
| B | PRO197 |
| B | GLY198 |
| B | GLY199 |
| B | THR200 |
| B | THR202 |
| B | ASP203 |
| B | MET204 |
| B | HOH410 |
| B | HOH431 |
| B | HOH456 |
| B | HOH458 |
| site_id | AC7 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL C 301 |
| Chain | Residue |
| A | GLU254 |
| C | HIS37 |
| C | ASN245 |
| C | PHE249 |
| C | HOH452 |
| C | HOH469 |
| C | HOH559 |
| C | HOH560 |
| site_id | AC8 |
| Number of Residues | 36 |
| Details | BINDING SITE FOR RESIDUE NAP C 302 |
| Chain | Residue |
| C | GLY25 |
| C | ARG28 |
| C | GLY29 |
| C | ILE30 |
| C | TYR49 |
| C | ALA50 |
| C | ASN51 |
| C | SER52 |
| C | ALA75 |
| C | ASP76 |
| C | ILE77 |
| C | ARG78 |
| C | ASN103 |
| C | SER104 |
| C | GLY105 |
| C | LEU126 |
| C | THR151 |
| C | SER152 |
| C | SER153 |
| C | TYR167 |
| C | LYS171 |
| C | PRO197 |
| C | GLY198 |
| C | GLY199 |
| C | THR200 |
| C | THR202 |
| C | ASP203 |
| C | MET204 |
| C | HOH401 |
| C | HOH412 |
| C | HOH416 |
| C | HOH427 |
| C | HOH449 |
| C | HOH457 |
| C | HOH495 |
| C | HOH496 |
| site_id | AC9 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL D 301 |
| Chain | Residue |
| A | ARG140 |
| B | LYS113 |
| B | ASP114 |
| B | HOH475 |
| D | THR220 |
| D | ALA221 |
| D | GLU222 |
| D | HOH514 |
| D | HOH526 |
| site_id | BC1 |
| Number of Residues | 31 |
| Details | BINDING SITE FOR RESIDUE NAP D 302 |
| Chain | Residue |
| D | GLY25 |
| D | ARG28 |
| D | GLY29 |
| D | ILE30 |
| D | ALA50 |
| D | ASN51 |
| D | SER52 |
| D | ALA75 |
| D | ASP76 |
| D | ILE77 |
| D | ASN103 |
| D | SER104 |
| D | GLY105 |
| D | LEU126 |
| D | THR151 |
| D | SER152 |
| D | SER153 |
| D | TYR167 |
| D | LYS171 |
| D | PRO197 |
| D | GLY198 |
| D | GLY199 |
| D | THR200 |
| D | THR202 |
| D | MET204 |
| D | HOH421 |
| D | HOH427 |
| D | HOH429 |
| D | HOH437 |
| D | HOH466 |
| D | HOH516 |
| site_id | BC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL E 301 |
| Chain | Residue |
| E | LYS19 |
| E | GLY145 |
| E | VAL251 |
| E | SER252 |
| E | LYS253 |
| E | HOH462 |
| E | HOH492 |
| site_id | BC3 |
| Number of Residues | 33 |
| Details | BINDING SITE FOR RESIDUE NAP E 302 |
| Chain | Residue |
| E | GLY25 |
| E | ARG28 |
| E | GLY29 |
| E | ILE30 |
| E | ALA50 |
| E | ASN51 |
| E | SER52 |
| E | ALA75 |
| E | ASP76 |
| E | ILE77 |
| E | ARG78 |
| E | ASN103 |
| E | SER104 |
| E | GLY105 |
| E | LEU126 |
| E | THR151 |
| E | SER152 |
| E | SER153 |
| E | TYR167 |
| E | LYS171 |
| E | PRO197 |
| E | GLY198 |
| E | GLY199 |
| E | THR200 |
| E | THR202 |
| E | MET204 |
| E | HOH441 |
| E | HOH443 |
| E | HOH455 |
| E | HOH471 |
| E | HOH487 |
| E | HOH511 |
| E | HOH526 |
| site_id | BC4 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL F 301 |
| Chain | Residue |
| F | GLY14 |
| F | HIS37 |
| F | ASN245 |
| F | PHE249 |
| F | HOH492 |
| F | HOH548 |
| H | GLU254 |
| H | HOH534 |
| site_id | BC5 |
| Number of Residues | 34 |
| Details | BINDING SITE FOR RESIDUE NAP F 302 |
| Chain | Residue |
| F | GLY25 |
| F | ARG28 |
| F | GLY29 |
| F | ILE30 |
| F | TYR49 |
| F | ALA50 |
| F | ASN51 |
| F | SER52 |
| F | ALA75 |
| F | ASP76 |
| F | ILE77 |
| F | ARG78 |
| F | ASN103 |
| F | SER104 |
| F | GLY105 |
| F | LEU126 |
| F | THR151 |
| F | SER152 |
| F | SER153 |
| F | TYR167 |
| F | LYS171 |
| F | PRO197 |
| F | GLY198 |
| F | GLY199 |
| F | THR200 |
| F | THR202 |
| F | MET204 |
| F | HOH405 |
| F | HOH410 |
| F | HOH411 |
| F | HOH436 |
| F | HOH443 |
| F | HOH484 |
| F | HOH553 |
| site_id | BC6 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL G 301 |
| Chain | Residue |
| G | LYS19 |
| G | GLY145 |
| G | GLY146 |
| G | VAL251 |
| G | SER252 |
| G | LYS253 |
| G | HOH479 |
| G | HOH545 |
| site_id | BC7 |
| Number of Residues | 33 |
| Details | BINDING SITE FOR RESIDUE NAP G 302 |
| Chain | Residue |
| G | GLY25 |
| G | ARG28 |
| G | GLY29 |
| G | ILE30 |
| G | ALA50 |
| G | ASN51 |
| G | SER52 |
| G | ALA75 |
| G | ASP76 |
| G | ILE77 |
| G | ARG78 |
| G | ASN103 |
| G | SER104 |
| G | GLY105 |
| G | LEU126 |
| G | THR151 |
| G | SER152 |
| G | SER153 |
| G | TYR167 |
| G | LYS171 |
| G | PRO197 |
| G | GLY198 |
| G | GLY199 |
| G | THR200 |
| G | THR202 |
| G | MET204 |
| G | HOH402 |
| G | HOH404 |
| G | HOH422 |
| G | HOH423 |
| G | HOH428 |
| G | HOH499 |
| G | HOH520 |
| site_id | BC8 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL H 301 |
| Chain | Residue |
| F | PRO13 |
| F | HOH492 |
| H | GLY14 |
| H | HIS37 |
| H | ASN245 |
| H | GLY248 |
| H | PHE249 |
| H | HOH534 |
| site_id | BC9 |
| Number of Residues | 33 |
| Details | BINDING SITE FOR RESIDUE NAP H 302 |
| Chain | Residue |
| H | GLY25 |
| H | ARG28 |
| H | GLY29 |
| H | ILE30 |
| H | ALA50 |
| H | ASN51 |
| H | SER52 |
| H | ALA75 |
| H | ASP76 |
| H | ILE77 |
| H | ARG78 |
| H | ASN103 |
| H | SER104 |
| H | GLY105 |
| H | LEU126 |
| H | THR151 |
| H | SER152 |
| H | SER153 |
| H | TYR167 |
| H | LYS171 |
| H | PRO197 |
| H | GLY198 |
| H | GLY199 |
| H | THR200 |
| H | THR202 |
| H | MET204 |
| H | HOH410 |
| H | HOH428 |
| H | HOH432 |
| H | HOH448 |
| H | HOH449 |
| H | HOH491 |
| H | HOH510 |
Functional Information from PROSITE/UniProt
| site_id | PS00061 |
| Number of Residues | 29 |
| Details | ADH_SHORT Short-chain dehydrogenases/reductases family signature. NtskdfsvpkHslYSGSKGAVdSFVrIFS |
| Chain | Residue | Details |
| A | ASN154-SER182 |
