3H02
2.15 Angstrom Resolution Crystal Structure of Naphthoate Synthase from Salmonella typhimurium.
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0005829 | cellular_component | cytosol |
| A | 0008935 | molecular_function | 1,4-dihydroxy-2-naphthoyl-CoA synthase activity |
| A | 0009234 | biological_process | menaquinone biosynthetic process |
| A | 0016829 | molecular_function | lyase activity |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0005829 | cellular_component | cytosol |
| B | 0008935 | molecular_function | 1,4-dihydroxy-2-naphthoyl-CoA synthase activity |
| B | 0009234 | biological_process | menaquinone biosynthetic process |
| B | 0016829 | molecular_function | lyase activity |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0005829 | cellular_component | cytosol |
| C | 0008935 | molecular_function | 1,4-dihydroxy-2-naphthoyl-CoA synthase activity |
| C | 0009234 | biological_process | menaquinone biosynthetic process |
| C | 0016829 | molecular_function | lyase activity |
| D | 0003824 | molecular_function | catalytic activity |
| D | 0005829 | cellular_component | cytosol |
| D | 0008935 | molecular_function | 1,4-dihydroxy-2-naphthoyl-CoA synthase activity |
| D | 0009234 | biological_process | menaquinone biosynthetic process |
| D | 0016829 | molecular_function | lyase activity |
| E | 0003824 | molecular_function | catalytic activity |
| E | 0005829 | cellular_component | cytosol |
| E | 0008935 | molecular_function | 1,4-dihydroxy-2-naphthoyl-CoA synthase activity |
| E | 0009234 | biological_process | menaquinone biosynthetic process |
| E | 0016829 | molecular_function | lyase activity |
| F | 0003824 | molecular_function | catalytic activity |
| F | 0005829 | cellular_component | cytosol |
| F | 0008935 | molecular_function | 1,4-dihydroxy-2-naphthoyl-CoA synthase activity |
| F | 0009234 | biological_process | menaquinone biosynthetic process |
| F | 0016829 | molecular_function | lyase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 A 286 |
| Chain | Residue |
| A | ILE174 |
| A | HOH589 |
| B | ILE174 |
| C | ILE174 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE BCT A 287 |
| Chain | Residue |
| A | PHE162 |
| A | TRP184 |
| A | GLY132 |
| A | GLY133 |
| A | GLN154 |
| A | THR155 |
| A | GLY156 |
| site_id | AC3 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE BCT B 286 |
| Chain | Residue |
| B | GLY132 |
| B | GLY133 |
| B | GLN154 |
| B | THR155 |
| B | GLY156 |
| B | PHE162 |
| B | ASP163 |
| B | TRP184 |
| B | HOH556 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE BCT C 286 |
| Chain | Residue |
| C | GLY132 |
| C | GLY133 |
| C | GLN154 |
| C | THR155 |
| C | GLY156 |
| C | PHE162 |
| C | TRP184 |
| C | HOH501 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE BCT D 286 |
| Chain | Residue |
| D | GLY132 |
| D | GLY133 |
| D | GLN154 |
| D | THR155 |
| D | GLY156 |
| D | PHE162 |
| D | TRP184 |
| site_id | AC6 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE BCT E 286 |
| Chain | Residue |
| E | GLY132 |
| E | GLY133 |
| E | GLN154 |
| E | THR155 |
| E | GLY156 |
| E | PHE162 |
| E | TRP184 |
| E | HOH591 |
| site_id | AC7 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE SO4 F 286 |
| Chain | Residue |
| D | ILE174 |
| D | VAL175 |
| D | GLY176 |
| E | ILE174 |
| E | VAL175 |
| E | GLY176 |
| F | ILE174 |
| F | VAL175 |
| F | GLY176 |
| F | HOH510 |
| F | HOH583 |
| site_id | AC8 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE BCT F 287 |
| Chain | Residue |
| F | GLY132 |
| F | GLY133 |
| F | GLN154 |
| F | THR155 |
| F | GLY156 |
| F | PHE162 |
| F | TRP184 |
| F | HOH630 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE BCT F 288 |
| Chain | Residue |
| F | GLU20 |
| F | TYR22 |
| F | GLN58 |
| F | HOH483 |
| F | HOH614 |
Functional Information from PROSITE/UniProt
| site_id | PS00166 |
| Number of Residues | 21 |
| Details | ENOYL_COA_HYDRATASE Enoyl-CoA hydratase/isomerase signature. VAmVAGysiGGGhvlhMmCDL |
| Chain | Residue | Details |
| A | VAL123-LEU143 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 48 |
| Details | Binding site: {"description":"in other chain","evidences":[{"source":"UniProtKB","id":"P0ABU0","evidenceCode":"ECO:0000250"},{"source":"HAMAP-Rule","id":"MF_01934","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01934","evidenceCode":"ECO:0000255"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"OCT-2009","submissionDatabase":"EMBL/GenBank/DDBJ databases","title":"2.15 angstrom resolution crystal structure of naphthoate synthase from Salmonella typhimurium.","authors":["Minasov G.","Wawrzak Z.","Skarina T.","Onopriyenko O.","Peterson S.N.","Savchenko A.","Anderson W.F."]}}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | Site: {"description":"Important for catalysis","evidences":[{"source":"UniProtKB","id":"P0ABU0","evidenceCode":"ECO:0000250"},{"source":"HAMAP-Rule","id":"MF_01934","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
