1GYR
Mutant form of enoyl thioester reductase from Candida tropicalis
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0006631 | biological_process | fatty acid metabolic process |
| A | 0006633 | biological_process | fatty acid biosynthetic process |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0019166 | molecular_function | trans-2-enoyl-CoA reductase (NADPH) activity |
| A | 0141148 | molecular_function | enoyl-[acyl-carrier-protein] reductase (NADPH) activity |
| B | 0005739 | cellular_component | mitochondrion |
| B | 0006631 | biological_process | fatty acid metabolic process |
| B | 0006633 | biological_process | fatty acid biosynthetic process |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0019166 | molecular_function | trans-2-enoyl-CoA reductase (NADPH) activity |
| B | 0141148 | molecular_function | enoyl-[acyl-carrier-protein] reductase (NADPH) activity |
| C | 0005739 | cellular_component | mitochondrion |
| C | 0006631 | biological_process | fatty acid metabolic process |
| C | 0006633 | biological_process | fatty acid biosynthetic process |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0019166 | molecular_function | trans-2-enoyl-CoA reductase (NADPH) activity |
| C | 0141148 | molecular_function | enoyl-[acyl-carrier-protein] reductase (NADPH) activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 A 1390 |
| Chain | Residue |
| A | GLY197 |
| A | GLY198 |
| A | THR199 |
| A | VAL220 |
| A | ILE221 |
| A | ARG222 |
| A | ARG224 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 A 1391 |
| Chain | Residue |
| A | ALA201 |
| A | LYS381 |
| A | HOH2053 |
| A | HOH2054 |
| A | PRO69 |
| A | ASN172 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 A 1392 |
| Chain | Residue |
| A | ARG285 |
| A | PRO307 |
| A | SER309 |
| A | HOH2055 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 B 1391 |
| Chain | Residue |
| B | GLY197 |
| B | GLY198 |
| B | THR199 |
| B | VAL220 |
| B | ILE221 |
| B | ARG222 |
| B | ARG224 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 B 1392 |
| Chain | Residue |
| B | PRO69 |
| B | ASN172 |
| B | ALA201 |
| B | LYS381 |
| B | HOH2042 |
| B | HOH2043 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 B 1393 |
| Chain | Residue |
| B | ARG285 |
| B | PRO307 |
| B | SER309 |
| site_id | AC7 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 C 1391 |
| Chain | Residue |
| C | GLY197 |
| C | GLY198 |
| C | THR199 |
| C | VAL220 |
| C | ILE221 |
| C | ARG222 |
| C | ARG224 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 C 1392 |
| Chain | Residue |
| C | PRO69 |
| C | ASN172 |
| C | ALA201 |
| C | LYS381 |
| C | HOH2068 |
| site_id | AC9 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 C 1393 |
| Chain | Residue |
| C | ARG285 |
| C | PRO307 |
| C | SER309 |
| site_id | BC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL A 1387 |
| Chain | Residue |
| A | GLY254 |
| A | LYS258 |
| A | LYS286 |
| A | HOH2052 |
| site_id | BC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL A 1388 |
| Chain | Residue |
| A | ARG224 |
| A | ASN226 |
| A | VAL230 |
| site_id | BC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL A 1389 |
| Chain | Residue |
| A | LEU227 |
| A | VAL242 |
| A | ILE243 |
| A | GLN247 |
| site_id | BC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL B 1387 |
| Chain | Residue |
| B | VAL242 |
| B | THR244 |
| B | GLN247 |
| B | HOH2041 |
| site_id | BC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL B 1388 |
| Chain | Residue |
| B | ASN248 |
| B | ASN249 |
| B | ARG251 |
| B | ARG285 |
| B | LYS286 |
| B | HOH2024 |
| site_id | BC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL B 1389 |
| Chain | Residue |
| B | ARG224 |
| B | ASN226 |
| B | VAL230 |
| site_id | BC7 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE GOL B 1390 |
| Chain | Residue |
| B | SER336 |
| B | ASN339 |
| site_id | BC8 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE GOL C 1387 |
| Chain | Residue |
| C | HIS34 |
| C | LYS85 |
| site_id | BC9 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL C 1388 |
| Chain | Residue |
| A | LYS235 |
| C | ARG224 |
| C | PRO225 |
| C | ASN226 |
| C | LEU227 |
| C | ASP228 |
| C | HOH2066 |
| site_id | CC1 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE GOL C 1389 |
| Chain | Residue |
| C | SER336 |
| C | ASN339 |
| site_id | CC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL C 1390 |
| Chain | Residue |
| C | LEU227 |
| C | VAL242 |
| C | GLN247 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 3 |
| Details | ACT_SITE: Proton donor => ECO:0000269|PubMed:25867044 |
| Chain | Residue | Details |
| A | ASN79 | |
| B | ASN79 | |
| C | ASN79 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 18 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:12614607, ECO:0000269|PubMed:12890667 |
| Chain | Residue | Details |
| A | ASN172 | |
| B | TYR296 | |
| B | PHE321 | |
| B | LYS381 | |
| C | ASN172 | |
| C | THR199 | |
| C | ARG222 | |
| C | TYR296 | |
| C | PHE321 | |
| C | LYS381 | |
| A | THR199 | |
| A | ARG222 | |
| A | TYR296 | |
| A | PHE321 | |
| A | LYS381 | |
| B | ASN172 | |
| B | THR199 | |
| B | ARG222 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1guf |
| Chain | Residue | Details |
| A | ASN79 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1guf |
| Chain | Residue | Details |
| B | ASN79 |
| site_id | CSA3 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1guf |
| Chain | Residue | Details |
| C | ASN79 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1guf |
| Chain | Residue | Details |
| A | ASN73 | |
| A | SER70 |
| site_id | CSA5 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1guf |
| Chain | Residue | Details |
| B | ASN73 | |
| B | SER70 |
| site_id | CSA6 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1guf |
| Chain | Residue | Details |
| C | ASN73 | |
| C | SER70 |
| site_id | MCSA1 |
| Number of Residues | 1 |
| Details | M-CSA 620 |
| Chain | Residue | Details |
| A | ASN79 | electrostatic stabiliser, increase electrophilicity |
| site_id | MCSA2 |
| Number of Residues | 1 |
| Details | M-CSA 620 |
| Chain | Residue | Details |
| B | ASN79 | electrostatic stabiliser, increase electrophilicity |
| site_id | MCSA3 |
| Number of Residues | 1 |
| Details | M-CSA 620 |
| Chain | Residue | Details |
| C | ASN79 | electrostatic stabiliser, increase electrophilicity |
