5H5X
Crystal structure of NADH bound carbonyl reductase from Streptomyces coelicolor
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0008202 | biological_process | steroid metabolic process |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0008202 | biological_process | steroid metabolic process |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0008202 | biological_process | steroid metabolic process |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0008202 | biological_process | steroid metabolic process |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0046872 | molecular_function | metal ion binding |
| E | 0000166 | molecular_function | nucleotide binding |
| E | 0008202 | biological_process | steroid metabolic process |
| E | 0016491 | molecular_function | oxidoreductase activity |
| E | 0046872 | molecular_function | metal ion binding |
| F | 0000166 | molecular_function | nucleotide binding |
| F | 0008202 | biological_process | steroid metabolic process |
| F | 0016491 | molecular_function | oxidoreductase activity |
| F | 0046872 | molecular_function | metal ion binding |
| G | 0000166 | molecular_function | nucleotide binding |
| G | 0008202 | biological_process | steroid metabolic process |
| G | 0016491 | molecular_function | oxidoreductase activity |
| G | 0046872 | molecular_function | metal ion binding |
| H | 0000166 | molecular_function | nucleotide binding |
| H | 0008202 | biological_process | steroid metabolic process |
| H | 0016491 | molecular_function | oxidoreductase activity |
| H | 0046872 | molecular_function | metal ion binding |
| I | 0000166 | molecular_function | nucleotide binding |
| I | 0008202 | biological_process | steroid metabolic process |
| I | 0016491 | molecular_function | oxidoreductase activity |
| I | 0046872 | molecular_function | metal ion binding |
| J | 0000166 | molecular_function | nucleotide binding |
| J | 0008202 | biological_process | steroid metabolic process |
| J | 0016491 | molecular_function | oxidoreductase activity |
| J | 0046872 | molecular_function | metal ion binding |
| K | 0000166 | molecular_function | nucleotide binding |
| K | 0008202 | biological_process | steroid metabolic process |
| K | 0016491 | molecular_function | oxidoreductase activity |
| K | 0046872 | molecular_function | metal ion binding |
| L | 0000166 | molecular_function | nucleotide binding |
| L | 0008202 | biological_process | steroid metabolic process |
| L | 0016491 | molecular_function | oxidoreductase activity |
| L | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 24 |
| Details | binding site for residue NAI A 301 |
| Chain | Residue |
| A | GLY26 |
| A | ASN103 |
| A | ALA104 |
| A | GLY105 |
| A | VAL155 |
| A | ALA156 |
| A | TYR170 |
| A | LYS174 |
| A | PRO200 |
| A | GLY201 |
| A | ILE203 |
| A | SER29 |
| A | THR205 |
| A | IPA302 |
| A | HOH418 |
| A | HOH444 |
| A | HOH450 |
| A | GLY30 |
| A | ILE31 |
| A | ASP50 |
| A | PHE51 |
| A | LEU75 |
| A | ASP76 |
| A | VAL77 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue IPA A 302 |
| Chain | Residue |
| A | SER157 |
| A | TYR170 |
| A | PHE202 |
| A | NAI301 |
| A | IPA303 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | binding site for residue IPA A 303 |
| Chain | Residue |
| A | SER167 |
| A | TYR170 |
| A | IPA302 |
| site_id | AC4 |
| Number of Residues | 26 |
| Details | binding site for residue NAI B 301 |
| Chain | Residue |
| B | GLY26 |
| B | ALA28 |
| B | SER29 |
| B | GLY30 |
| B | ILE31 |
| B | ASP50 |
| B | PHE51 |
| B | LEU75 |
| B | ASP76 |
| B | VAL77 |
| B | ASN103 |
| B | ALA104 |
| B | GLY105 |
| B | THR127 |
| B | VAL155 |
| B | ALA156 |
| B | SER157 |
| B | TYR170 |
| B | LYS174 |
| B | PRO200 |
| B | GLY201 |
| B | PHE202 |
| B | ILE203 |
| B | IPA302 |
| B | HOH448 |
| B | HOH454 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | binding site for residue IPA B 302 |
| Chain | Residue |
| B | SER157 |
| B | TYR170 |
| B | PHE202 |
| B | NAI301 |
| B | IPA303 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | binding site for residue IPA B 303 |
| Chain | Residue |
| B | GLY107 |
| B | SER167 |
| B | TYR170 |
| B | IPA302 |
| site_id | AC7 |
| Number of Residues | 23 |
| Details | binding site for residue NAI C 301 |
| Chain | Residue |
| C | GLY26 |
| C | SER29 |
| C | GLY30 |
| C | ILE31 |
| C | ASP50 |
| C | PHE51 |
| C | LEU75 |
| C | ASP76 |
| C | VAL77 |
| C | ASN103 |
| C | VAL155 |
| C | ALA156 |
| C | TYR170 |
| C | LYS174 |
| C | PRO200 |
| C | GLY201 |
| C | ILE203 |
| C | THR205 |
| C | IPA302 |
| C | HOH404 |
| C | HOH414 |
| C | HOH416 |
| C | HOH420 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | binding site for residue IPA C 302 |
| Chain | Residue |
| C | SER157 |
| C | TYR170 |
| C | PHE202 |
| C | NAI301 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | binding site for residue MG C 303 |
| Chain | Residue |
| C | HOH442 |
| A | VAL263 |
| A | HOH415 |
| A | HOH423 |
| A | HOH476 |
| C | VAL263 |
| site_id | AD1 |
| Number of Residues | 2 |
| Details | binding site for residue IPA C 304 |
| Chain | Residue |
| C | SER167 |
| C | TYR170 |
| site_id | AD2 |
| Number of Residues | 27 |
| Details | binding site for residue NAI D 301 |
| Chain | Residue |
| D | GLY26 |
| D | SER29 |
| D | GLY30 |
| D | ILE31 |
| D | ASP50 |
| D | PHE51 |
| D | LEU75 |
| D | ASP76 |
| D | VAL77 |
| D | ASN103 |
| D | ALA104 |
| D | GLY105 |
| D | THR127 |
| D | VAL155 |
| D | ALA156 |
| D | TYR170 |
| D | LYS174 |
| D | PRO200 |
| D | GLY201 |
| D | ILE203 |
| D | THR205 |
| D | IPA302 |
| D | HOH404 |
| D | HOH405 |
| D | HOH433 |
| D | HOH440 |
| D | HOH452 |
| site_id | AD3 |
| Number of Residues | 4 |
| Details | binding site for residue IPA D 302 |
| Chain | Residue |
| D | SER157 |
| D | TYR170 |
| D | PHE202 |
| D | NAI301 |
| site_id | AD4 |
| Number of Residues | 6 |
| Details | binding site for residue MG D 303 |
| Chain | Residue |
| B | VAL263 |
| B | HOH409 |
| B | HOH413 |
| B | HOH423 |
| B | HOH475 |
| D | VAL263 |
| site_id | AD5 |
| Number of Residues | 29 |
| Details | binding site for residue NAI E 301 |
| Chain | Residue |
| E | GLY26 |
| E | SER29 |
| E | GLY30 |
| E | ILE31 |
| E | ASP50 |
| E | PHE51 |
| E | LEU75 |
| E | ASP76 |
| E | VAL77 |
| E | ASN103 |
| E | ALA104 |
| E | GLY105 |
| E | THR127 |
| E | VAL155 |
| E | ALA156 |
| E | SER157 |
| E | TYR170 |
| E | LYS174 |
| E | PRO200 |
| E | GLY201 |
| E | PHE202 |
| E | ILE203 |
| E | THR205 |
| E | PRO206 |
| E | IPA303 |
| E | HOH405 |
| E | HOH440 |
| E | HOH450 |
| E | HOH453 |
| site_id | AD6 |
| Number of Residues | 6 |
| Details | binding site for residue MG E 302 |
| Chain | Residue |
| E | VAL263 |
| G | VAL263 |
| G | HOH424 |
| G | HOH432 |
| G | HOH433 |
| G | HOH460 |
| site_id | AD7 |
| Number of Residues | 5 |
| Details | binding site for residue IPA E 303 |
| Chain | Residue |
| E | SER157 |
| E | TYR170 |
| E | PHE202 |
| E | NAI301 |
| E | IPA304 |
| site_id | AD8 |
| Number of Residues | 3 |
| Details | binding site for residue IPA E 304 |
| Chain | Residue |
| E | SER167 |
| E | TYR170 |
| E | IPA303 |
| site_id | AD9 |
| Number of Residues | 24 |
| Details | binding site for residue NAI F 301 |
| Chain | Residue |
| F | GLY26 |
| F | SER29 |
| F | GLY30 |
| F | ILE31 |
| F | ASP50 |
| F | PHE51 |
| F | LEU75 |
| F | ASP76 |
| F | VAL77 |
| F | ASN103 |
| F | ALA104 |
| F | GLY105 |
| F | VAL155 |
| F | ALA156 |
| F | TYR170 |
| F | LYS174 |
| F | PRO200 |
| F | GLY201 |
| F | ILE203 |
| F | THR205 |
| F | IPA302 |
| F | HOH414 |
| F | HOH420 |
| F | HOH423 |
| site_id | AE1 |
| Number of Residues | 4 |
| Details | binding site for residue IPA F 302 |
| Chain | Residue |
| F | SER157 |
| F | TYR170 |
| F | PHE202 |
| F | NAI301 |
| site_id | AE2 |
| Number of Residues | 3 |
| Details | binding site for residue IPA F 303 |
| Chain | Residue |
| F | SER167 |
| F | TYR170 |
| F | HOH456 |
| site_id | AE3 |
| Number of Residues | 21 |
| Details | binding site for residue NAI G 301 |
| Chain | Residue |
| G | GLY26 |
| G | SER29 |
| G | GLY30 |
| G | ILE31 |
| G | ASP50 |
| G | PHE51 |
| G | LEU75 |
| G | ASP76 |
| G | VAL77 |
| G | ASN103 |
| G | ALA104 |
| G | GLY105 |
| G | VAL155 |
| G | ALA156 |
| G | TYR170 |
| G | LYS174 |
| G | PRO200 |
| G | GLY201 |
| G | ILE203 |
| G | IPA302 |
| G | HOH448 |
| site_id | AE4 |
| Number of Residues | 6 |
| Details | binding site for residue IPA G 302 |
| Chain | Residue |
| G | SER157 |
| G | LEU159 |
| G | TYR170 |
| G | PHE202 |
| G | NAI301 |
| G | IPA303 |
| site_id | AE5 |
| Number of Residues | 3 |
| Details | binding site for residue IPA G 303 |
| Chain | Residue |
| G | GLY107 |
| G | SER167 |
| G | IPA302 |
| site_id | AE6 |
| Number of Residues | 24 |
| Details | binding site for residue NAI H 301 |
| Chain | Residue |
| H | GLY26 |
| H | SER29 |
| H | GLY30 |
| H | ILE31 |
| H | ASP50 |
| H | PHE51 |
| H | LEU75 |
| H | ASP76 |
| H | VAL77 |
| H | THR78 |
| H | ASN103 |
| H | ALA104 |
| H | GLY105 |
| H | VAL155 |
| H | ALA156 |
| H | TYR170 |
| H | LYS174 |
| H | PRO200 |
| H | GLY201 |
| H | ILE203 |
| H | THR205 |
| H | IPA303 |
| H | HOH414 |
| H | HOH440 |
| site_id | AE7 |
| Number of Residues | 6 |
| Details | binding site for residue MG H 302 |
| Chain | Residue |
| F | VAL263 |
| F | HOH418 |
| H | VAL263 |
| H | HOH421 |
| H | HOH426 |
| H | HOH451 |
| site_id | AE8 |
| Number of Residues | 6 |
| Details | binding site for residue IPA H 303 |
| Chain | Residue |
| H | SER157 |
| H | LEU159 |
| H | TYR170 |
| H | PHE202 |
| H | NAI301 |
| H | IPA304 |
| site_id | AE9 |
| Number of Residues | 5 |
| Details | binding site for residue IPA H 304 |
| Chain | Residue |
| H | GLY107 |
| H | GLY108 |
| H | SER167 |
| H | TYR170 |
| H | IPA303 |
| site_id | AF1 |
| Number of Residues | 24 |
| Details | binding site for residue NAI I 301 |
| Chain | Residue |
| I | GLY26 |
| I | ALA28 |
| I | SER29 |
| I | GLY30 |
| I | ILE31 |
| I | ASP50 |
| I | PHE51 |
| I | LEU75 |
| I | ASP76 |
| I | VAL77 |
| I | ASN103 |
| I | ALA104 |
| I | GLY105 |
| I | VAL155 |
| I | ALA156 |
| I | SER157 |
| I | TYR170 |
| I | LYS174 |
| I | PRO200 |
| I | GLY201 |
| I | ILE203 |
| I | THR205 |
| I | IPA304 |
| I | HOH404 |
| site_id | AF2 |
| Number of Residues | 5 |
| Details | binding site for residue MG I 302 |
| Chain | Residue |
| I | VAL263 |
| I | HOH414 |
| K | VAL263 |
| K | HOH404 |
| K | HOH456 |
| site_id | AF3 |
| Number of Residues | 4 |
| Details | binding site for residue IPA I 303 |
| Chain | Residue |
| I | GLY107 |
| I | SER167 |
| I | TYR170 |
| I | IPA304 |
| site_id | AF4 |
| Number of Residues | 5 |
| Details | binding site for residue IPA I 304 |
| Chain | Residue |
| I | SER157 |
| I | TYR170 |
| I | PHE202 |
| I | NAI301 |
| I | IPA303 |
| site_id | AF5 |
| Number of Residues | 21 |
| Details | binding site for residue NAI J 301 |
| Chain | Residue |
| J | GLY26 |
| J | SER29 |
| J | GLY30 |
| J | ILE31 |
| J | ASP50 |
| J | PHE51 |
| J | LEU75 |
| J | ASP76 |
| J | VAL77 |
| J | ASN103 |
| J | GLY105 |
| J | VAL155 |
| J | ALA156 |
| J | SER157 |
| J | TYR170 |
| J | LYS174 |
| J | PRO200 |
| J | GLY201 |
| J | ILE203 |
| J | THR205 |
| J | IPA302 |
| site_id | AF6 |
| Number of Residues | 3 |
| Details | binding site for residue IPA J 302 |
| Chain | Residue |
| J | SER157 |
| J | TYR170 |
| J | NAI301 |
| site_id | AF7 |
| Number of Residues | 24 |
| Details | binding site for residue NAI K 301 |
| Chain | Residue |
| K | GLY26 |
| K | SER29 |
| K | ILE31 |
| K | ASP50 |
| K | PHE51 |
| K | LEU75 |
| K | ASP76 |
| K | VAL77 |
| K | ASN103 |
| K | ALA104 |
| K | GLY105 |
| K | THR127 |
| K | VAL155 |
| K | ALA156 |
| K | SER157 |
| K | TYR170 |
| K | LYS174 |
| K | PRO200 |
| K | GLY201 |
| K | ILE203 |
| K | IPA303 |
| K | HOH424 |
| K | HOH436 |
| K | HOH473 |
| site_id | AF8 |
| Number of Residues | 3 |
| Details | binding site for residue IPA K 302 |
| Chain | Residue |
| K | SER167 |
| K | TYR170 |
| K | IPA303 |
| site_id | AF9 |
| Number of Residues | 5 |
| Details | binding site for residue IPA K 303 |
| Chain | Residue |
| K | SER157 |
| K | LEU159 |
| K | TYR170 |
| K | NAI301 |
| K | IPA302 |
| site_id | AG1 |
| Number of Residues | 22 |
| Details | binding site for residue NAI L 301 |
| Chain | Residue |
| L | GLY26 |
| L | SER29 |
| L | GLY30 |
| L | ILE31 |
| L | ASP50 |
| L | PHE51 |
| L | LEU75 |
| L | ASP76 |
| L | VAL77 |
| L | ASN103 |
| L | ALA104 |
| L | GLY105 |
| L | VAL155 |
| L | ALA156 |
| L | TYR170 |
| L | LYS174 |
| L | PRO200 |
| L | GLY201 |
| L | ILE203 |
| L | IPA304 |
| L | HOH414 |
| L | HOH418 |
| site_id | AG2 |
| Number of Residues | 6 |
| Details | binding site for residue MG L 302 |
| Chain | Residue |
| J | VAL263 |
| J | HOH403 |
| J | HOH420 |
| J | HOH460 |
| J | HOH468 |
| L | VAL263 |
| site_id | AG3 |
| Number of Residues | 5 |
| Details | binding site for residue IPA L 303 |
| Chain | Residue |
| L | GLY107 |
| L | GLY108 |
| L | SER167 |
| L | TYR170 |
| L | IPA304 |
| site_id | AG4 |
| Number of Residues | 5 |
| Details | binding site for residue IPA L 304 |
| Chain | Residue |
| L | SER157 |
| L | TYR170 |
| L | PHE202 |
| L | NAI301 |
| L | IPA303 |
Functional Information from PROSITE/UniProt
| site_id | PS00061 |
| Number of Residues | 29 |
| Details | ADH_SHORT Short-chain dehydrogenases/reductases family signature. SilgsvgfagSpaYVAAKHGVvGLTkAAA |
| Chain | Residue | Details |
| A | SER157-ALA185 |
