3WY0
The I375W mutant of CsyB complexed with CoA-SH
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0009058 | biological_process | biosynthetic process |
A | 0016210 | molecular_function | naringenin-chalcone synthase activity |
A | 0016746 | molecular_function | acyltransferase activity |
A | 0016747 | molecular_function | acyltransferase activity, transferring groups other than amino-acyl groups |
A | 0030639 | biological_process | polyketide biosynthetic process |
A | 0034083 | cellular_component | type III polyketide synthase complex |
A | 0044550 | biological_process | secondary metabolite biosynthetic process |
A | 0090439 | molecular_function | tetraketide alpha-pyrone synthase activity |
B | 0009058 | biological_process | biosynthetic process |
B | 0016210 | molecular_function | naringenin-chalcone synthase activity |
B | 0016746 | molecular_function | acyltransferase activity |
B | 0016747 | molecular_function | acyltransferase activity, transferring groups other than amino-acyl groups |
B | 0030639 | biological_process | polyketide biosynthetic process |
B | 0034083 | cellular_component | type III polyketide synthase complex |
B | 0044550 | biological_process | secondary metabolite biosynthetic process |
B | 0090439 | molecular_function | tetraketide alpha-pyrone synthase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 20 |
Details | BINDING SITE FOR RESIDUE COA A 401 |
Chain | Residue |
A | LYS50 |
A | ILE271 |
A | GLY312 |
A | GLY313 |
A | TYR314 |
A | ALA315 |
A | HOH531 |
A | HOH563 |
A | HOH604 |
A | HOH677 |
A | HOH714 |
A | ILE54 |
A | HOH773 |
A | LYS57 |
A | THR58 |
A | ARG59 |
A | VAL208 |
A | LEU212 |
A | ILE267 |
A | LYS269 |
site_id | AC2 |
Number of Residues | 23 |
Details | BINDING SITE FOR RESIDUE COA B 401 |
Chain | Residue |
B | LYS50 |
B | ILE54 |
B | LYS57 |
B | THR58 |
B | VAL208 |
B | LEU212 |
B | ILE267 |
B | LYS269 |
B | ILE271 |
B | GLY312 |
B | GLY313 |
B | TYR314 |
B | ALA315 |
B | HOH545 |
B | HOH561 |
B | HOH622 |
B | HOH644 |
B | HOH675 |
B | HOH730 |
B | HOH756 |
B | HOH768 |
B | HOH780 |
B | HOH821 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Nucleophile => ECO:0000255|PROSITE-ProRule:PRU10023, ECO:0000269|PubMed:25564614 |
Chain | Residue | Details |
A | CYS155 | |
B | CYS155 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | ACT_SITE: ACT_SITE => ECO:0000269|PubMed:25564614 |
Chain | Residue | Details |
A | HIS377 | |
B | HIS377 |
site_id | SWS_FT_FI3 |
Number of Residues | 10 |
Details | BINDING: BINDING => ECO:0000269|PubMed:25564614, ECO:0007744|PDB:3WXY |
Chain | Residue | Details |
A | LYS50 | |
B | ALA315 | |
A | ILE267 | |
A | GLY312 | |
A | TYR314 | |
A | ALA315 | |
B | LYS50 | |
B | ILE267 | |
B | GLY312 | |
B | TYR314 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:P30074 |
Chain | Residue | Details |
A | GLY214 | |
B | GLY214 |