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 |