4C3Y
Crystal structure of 3-ketosteroid delta1-dehydrogenase from Rhodococcus erythropolis SQ1 in complex with 1,4-androstadiene-3,17- dione
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 | 0033765 | molecular_function | steroid dehydrogenase activity, acting on the CH-CH group of donors |
A | 0047571 | molecular_function | 3-oxosteroid 1-dehydrogenase activity |
B | 0000166 | molecular_function | nucleotide binding |
B | 0008202 | biological_process | steroid metabolic process |
B | 0016491 | molecular_function | oxidoreductase activity |
B | 0033765 | molecular_function | steroid dehydrogenase activity, acting on the CH-CH group of donors |
B | 0047571 | molecular_function | 3-oxosteroid 1-dehydrogenase activity |
C | 0000166 | molecular_function | nucleotide binding |
C | 0008202 | biological_process | steroid metabolic process |
C | 0016491 | molecular_function | oxidoreductase activity |
C | 0033765 | molecular_function | steroid dehydrogenase activity, acting on the CH-CH group of donors |
C | 0047571 | molecular_function | 3-oxosteroid 1-dehydrogenase activity |
D | 0000166 | molecular_function | nucleotide binding |
D | 0008202 | biological_process | steroid metabolic process |
D | 0016491 | molecular_function | oxidoreductase activity |
D | 0033765 | molecular_function | steroid dehydrogenase activity, acting on the CH-CH group of donors |
D | 0047571 | molecular_function | 3-oxosteroid 1-dehydrogenase activity |
E | 0000166 | molecular_function | nucleotide binding |
E | 0008202 | biological_process | steroid metabolic process |
E | 0016491 | molecular_function | oxidoreductase activity |
E | 0033765 | molecular_function | steroid dehydrogenase activity, acting on the CH-CH group of donors |
E | 0047571 | molecular_function | 3-oxosteroid 1-dehydrogenase activity |
F | 0000166 | molecular_function | nucleotide binding |
F | 0008202 | biological_process | steroid metabolic process |
F | 0016491 | molecular_function | oxidoreductase activity |
F | 0033765 | molecular_function | steroid dehydrogenase activity, acting on the CH-CH group of donors |
F | 0047571 | molecular_function | 3-oxosteroid 1-dehydrogenase activity |
G | 0000166 | molecular_function | nucleotide binding |
G | 0008202 | biological_process | steroid metabolic process |
G | 0016491 | molecular_function | oxidoreductase activity |
G | 0033765 | molecular_function | steroid dehydrogenase activity, acting on the CH-CH group of donors |
G | 0047571 | molecular_function | 3-oxosteroid 1-dehydrogenase activity |
H | 0000166 | molecular_function | nucleotide binding |
H | 0008202 | biological_process | steroid metabolic process |
H | 0016491 | molecular_function | oxidoreductase activity |
H | 0033765 | molecular_function | steroid dehydrogenase activity, acting on the CH-CH group of donors |
H | 0047571 | molecular_function | 3-oxosteroid 1-dehydrogenase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 34 |
Details | BINDING SITE FOR RESIDUE FAD A 551 |
Chain | Residue |
A | VAL13 |
A | THR45 |
A | SER46 |
A | SER49 |
A | GLY50 |
A | ALA51 |
A | SER52 |
A | SER193 |
A | VAL194 |
A | LEU195 |
A | ALA229 |
A | GLY14 |
A | GLY230 |
A | MET252 |
A | ALA257 |
A | ASN258 |
A | ASP261 |
A | LEU447 |
A | ASN477 |
A | GLY491 |
A | PRO493 |
A | LEU494 |
A | GLY16 |
A | ANB601 |
A | HOH2003 |
A | HOH2004 |
A | HOH2010 |
A | HOH2133 |
A | LEU36 |
A | GLU37 |
A | LYS38 |
A | THR39 |
A | GLY43 |
A | GLY44 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE NA A 561 |
Chain | Residue |
A | ASP154 |
A | GLN155 |
A | GLN160 |
B | ASP154 |
B | GLN155 |
B | GLN160 |
site_id | AC3 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE PG4 A 581 |
Chain | Residue |
A | PRO139 |
A | ALA146 |
A | GLY147 |
A | HIS162 |
A | ALA163 |
A | PRO164 |
A | GLY165 |
A | HOH2225 |
A | HOH2227 |
B | ARG299 |
B | GLU345 |
site_id | AC4 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE ANB A 601 |
Chain | Residue |
A | PHE116 |
A | TYR318 |
A | TYR487 |
A | PRO490 |
A | GLY491 |
A | FAD551 |
B | PG4581 |
site_id | AC5 |
Number of Residues | 36 |
Details | BINDING SITE FOR RESIDUE FAD B 551 |
Chain | Residue |
B | VAL13 |
B | GLY14 |
B | GLY16 |
B | LEU36 |
B | GLU37 |
B | LYS38 |
B | GLY43 |
B | GLY44 |
B | THR45 |
B | SER46 |
B | TYR48 |
B | SER49 |
B | GLY50 |
B | ALA51 |
B | SER52 |
B | SER193 |
B | VAL194 |
B | LEU195 |
B | ALA229 |
B | GLY230 |
B | MET252 |
B | ALA257 |
B | ASN258 |
B | ASP261 |
B | TRP280 |
B | LEU447 |
B | ASN477 |
B | GLY491 |
B | PRO493 |
B | LEU494 |
B | ANB601 |
B | HOH2003 |
B | HOH2004 |
B | HOH2085 |
B | HOH2088 |
B | HOH2100 |
site_id | AC6 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE PG4 B 581 |
Chain | Residue |
B | GLY165 |
B | HOH2200 |
A | ANB601 |
B | PRO139 |
B | HIS162 |
B | ALA163 |
B | PRO164 |
site_id | AC7 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE ANB B 601 |
Chain | Residue |
A | PRO164 |
B | PHE116 |
B | TYR318 |
B | TYR487 |
B | PRO490 |
B | GLY491 |
B | FAD551 |
B | HOH2201 |
site_id | AC8 |
Number of Residues | 34 |
Details | BINDING SITE FOR RESIDUE FAD C 551 |
Chain | Residue |
C | VAL13 |
C | GLY14 |
C | GLY16 |
C | LEU36 |
C | GLU37 |
C | LYS38 |
C | THR39 |
C | GLY43 |
C | GLY44 |
C | THR45 |
C | SER46 |
C | SER49 |
C | GLY50 |
C | ALA51 |
C | SER52 |
C | SER193 |
C | VAL194 |
C | LEU195 |
C | ALA229 |
C | GLY230 |
C | MET252 |
C | ALA257 |
C | ASN258 |
C | ASP261 |
C | LEU447 |
C | ASN477 |
C | GLY491 |
C | PRO493 |
C | LEU494 |
C | ANB601 |
C | HOH2003 |
C | HOH2004 |
C | HOH2007 |
C | HOH2078 |
site_id | AC9 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE NA C 561 |
Chain | Residue |
C | ASP154 |
C | GLN155 |
C | GLN160 |
D | ASP154 |
D | GLN155 |
D | GLN160 |
site_id | BC1 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE ANB C 601 |
Chain | Residue |
C | PHE116 |
C | TYR318 |
C | TYR487 |
C | PRO490 |
C | GLY491 |
C | FAD551 |
C | HOH2139 |
D | PRO164 |
site_id | BC2 |
Number of Residues | 34 |
Details | BINDING SITE FOR RESIDUE FAD D 551 |
Chain | Residue |
D | VAL13 |
D | GLY14 |
D | GLY16 |
D | LEU36 |
D | GLU37 |
D | LYS38 |
D | GLY43 |
D | GLY44 |
D | THR45 |
D | SER46 |
D | TYR48 |
D | SER49 |
D | GLY50 |
D | ALA51 |
D | SER52 |
D | SER193 |
D | VAL194 |
D | LEU195 |
D | ALA229 |
D | GLY230 |
D | MET252 |
D | ALA257 |
D | ASN258 |
D | ASP261 |
D | LEU447 |
D | ASN477 |
D | GLY491 |
D | PRO493 |
D | LEU494 |
D | ANB601 |
D | HOH2004 |
D | HOH2005 |
D | HOH2008 |
D | HOH2080 |
site_id | BC3 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE PG4 D 581 |
Chain | Residue |
C | ARG299 |
D | PRO139 |
D | ALA146 |
D | HIS162 |
D | ALA163 |
D | PRO164 |
D | GLY165 |
D | HOH2180 |
site_id | BC4 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE ANB D 601 |
Chain | Residue |
C | PRO164 |
D | SER52 |
D | TYR318 |
D | TYR487 |
D | PRO490 |
D | GLY491 |
D | FAD551 |
site_id | BC5 |
Number of Residues | 34 |
Details | BINDING SITE FOR RESIDUE FAD E 551 |
Chain | Residue |
E | VAL13 |
E | GLY14 |
E | GLY16 |
E | LEU36 |
E | GLU37 |
E | LYS38 |
E | THR39 |
E | GLY43 |
E | GLY44 |
E | THR45 |
E | SER46 |
E | TYR48 |
E | SER49 |
E | GLY50 |
E | ALA51 |
E | SER52 |
E | LEU153 |
E | SER193 |
E | LEU195 |
E | ALA229 |
E | GLY230 |
E | MET252 |
E | ALA257 |
E | ASN258 |
E | ASP261 |
E | LEU447 |
E | ASN477 |
E | GLY491 |
E | PRO493 |
E | LEU494 |
E | ANB601 |
E | HOH2001 |
E | HOH2002 |
E | HOH2100 |
site_id | BC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE NA E 561 |
Chain | Residue |
E | ASP154 |
E | GLN155 |
E | GLN160 |
F | ASP154 |
F | GLN155 |
F | GLN160 |
site_id | BC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE PG4 E 581 |
Chain | Residue |
E | PRO139 |
E | GLY143 |
E | ALA163 |
E | PRO164 |
site_id | BC8 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE ANB E 601 |
Chain | Residue |
E | PHE116 |
E | TYR119 |
E | TYR318 |
E | TYR487 |
E | PRO490 |
E | GLY491 |
E | FAD551 |
E | HOH2190 |
F | PRO164 |
site_id | BC9 |
Number of Residues | 34 |
Details | BINDING SITE FOR RESIDUE FAD F 551 |
Chain | Residue |
F | VAL13 |
F | GLY14 |
F | GLY16 |
F | LEU36 |
F | GLU37 |
F | LYS38 |
F | GLY43 |
F | GLY44 |
F | THR45 |
F | SER46 |
F | SER49 |
F | GLY50 |
F | ALA51 |
F | SER52 |
F | SER193 |
F | VAL194 |
F | LEU195 |
F | ALA229 |
F | GLY230 |
F | MET252 |
F | ALA257 |
F | ASN258 |
F | ASP261 |
F | LEU447 |
F | ASN477 |
F | GLY491 |
F | PRO493 |
F | LEU494 |
F | ANB601 |
F | HOH2003 |
F | HOH2004 |
F | HOH2007 |
F | HOH2009 |
F | HOH2074 |
site_id | CC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE PG4 F 581 |
Chain | Residue |
F | PRO139 |
F | HIS162 |
F | ALA163 |
F | PRO164 |
F | GLY165 |
F | HOH2134 |
site_id | CC2 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE ANB F 601 |
Chain | Residue |
E | PRO164 |
F | SER52 |
F | PHE116 |
F | TYR318 |
F | TYR487 |
F | PRO490 |
F | GLY491 |
F | FAD551 |
site_id | CC3 |
Number of Residues | 35 |
Details | BINDING SITE FOR RESIDUE FAD G 551 |
Chain | Residue |
G | VAL13 |
G | GLY14 |
G | GLY16 |
G | LEU36 |
G | GLU37 |
G | LYS38 |
G | GLY43 |
G | GLY44 |
G | THR45 |
G | SER46 |
G | TYR48 |
G | SER49 |
G | GLY50 |
G | ALA51 |
G | SER52 |
G | SER193 |
G | VAL194 |
G | LEU195 |
G | ALA229 |
G | GLY230 |
G | MET252 |
G | ALA257 |
G | ASN258 |
G | ASP261 |
G | LEU447 |
G | ASN477 |
G | GLY491 |
G | PRO493 |
G | LEU494 |
G | ANB601 |
G | HOH2002 |
G | HOH2003 |
G | HOH2008 |
G | HOH2085 |
G | HOH2100 |
site_id | CC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE NA G 561 |
Chain | Residue |
G | ASP154 |
G | GLN155 |
G | GLN160 |
H | ASP154 |
H | GLN155 |
H | GLN160 |
site_id | CC5 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE ANB G 601 |
Chain | Residue |
G | PHE116 |
G | TYR318 |
G | TYR487 |
G | PRO490 |
G | GLY491 |
G | FAD551 |
H | PRO164 |
site_id | CC6 |
Number of Residues | 35 |
Details | BINDING SITE FOR RESIDUE FAD H 551 |
Chain | Residue |
H | VAL13 |
H | GLY14 |
H | GLY16 |
H | LEU36 |
H | GLU37 |
H | LYS38 |
H | THR39 |
H | GLY43 |
H | GLY44 |
H | THR45 |
H | SER46 |
H | SER49 |
H | GLY50 |
H | ALA51 |
H | SER52 |
H | SER193 |
H | VAL194 |
H | LEU195 |
H | ALA229 |
H | GLY230 |
H | MET252 |
H | ALA257 |
H | ASN258 |
H | ASP261 |
H | LEU447 |
H | GLY476 |
H | ASN477 |
H | GLY491 |
H | PRO493 |
H | LEU494 |
H | ANB601 |
H | HOH2004 |
H | HOH2005 |
H | HOH2075 |
H | HOH2086 |
site_id | CC7 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE PG4 H 581 |
Chain | Residue |
G | GLU345 |
G | ILE352 |
H | PRO139 |
H | HIS162 |
H | ALA163 |
H | PRO164 |
H | GLY165 |
site_id | CC8 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE ANB H 601 |
Chain | Residue |
H | SER52 |
H | PHE294 |
H | TYR318 |
H | TYR487 |
H | PRO490 |
H | GLY491 |
H | FAD551 |