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 |