2FQ1
Crystal structure of the two-domain non-ribosomal peptide synthetase EntB containing isochorismate lyase and aryl-carrier protein domains
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0005515 | molecular_function | protein binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0008908 | molecular_function | isochorismatase activity |
| A | 0009239 | biological_process | enterobactin biosynthetic process |
| A | 0016765 | molecular_function | transferase activity, transferring alkyl or aryl (other than methyl) groups |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016874 | molecular_function | ligase activity |
| A | 0031177 | molecular_function | phosphopantetheine binding |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0047527 | molecular_function | 2,3-dihydroxybenzoate-serine ligase activity |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0005515 | molecular_function | protein binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0005886 | cellular_component | plasma membrane |
| B | 0008908 | molecular_function | isochorismatase activity |
| B | 0009239 | biological_process | enterobactin biosynthetic process |
| B | 0016765 | molecular_function | transferase activity, transferring alkyl or aryl (other than methyl) groups |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0016874 | molecular_function | ligase activity |
| B | 0031177 | molecular_function | phosphopantetheine binding |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0047527 | molecular_function | 2,3-dihydroxybenzoate-serine ligase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG B 991 |
| Chain | Residue |
| A | ASP240 |
| A | HOH1095 |
| B | GLN69 |
| B | HOH1043 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG A 992 |
| Chain | Residue |
| A | GLU185 |
| B | HOH1055 |
| B | HOH1056 |
| site_id | AC3 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE MG A 993 |
| Chain | Residue |
| A | ASP110 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG B 994 |
| Chain | Residue |
| B | HOH1047 |
| B | HOH1052 |
| B | HOH1100 |
| B | ASP110 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG B 995 |
| Chain | Residue |
| B | HIS15 |
| B | HOH1008 |
| B | HOH1103 |
| site_id | AC6 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE MG A 996 |
| Chain | Residue |
| A | HOH1016 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG A 997 |
| Chain | Residue |
| A | ASP227 |
| A | GLY242 |
| A | ASP244 |
| A | HOH1056 |
| A | HOH1067 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG A 998 |
| Chain | Residue |
| A | GLN69 |
| A | HOH1057 |
| A | HOH1058 |
| A | HOH1111 |
| B | GLU228 |
| B | ASP240 |
| site_id | AC9 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL B 950 |
| Chain | Residue |
| B | TYR152 |
| B | ILE155 |
| B | GLY156 |
| site_id | BC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL A 951 |
| Chain | Residue |
| A | TYR152 |
| A | ILE155 |
| A | GLY156 |
| site_id | BC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO A 800 |
| Chain | Residue |
| A | THR159 |
| A | TYR192 |
| B | THR159 |
| B | THR162 |
| B | TYR192 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:16632253, ECO:0007744|PDB:2FQ1 |
| Chain | Residue | Details |
| A | ASP227 | |
| A | GLY242 | |
| A | ASP244 | |
| B | ASP227 | |
| B | GLY242 | |
| B | ASP244 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | MOD_RES: O-(pantetheine 4'-phosphoryl)serine => ECO:0000269|PubMed:22365602, ECO:0007744|PDB:3RG2 |
| Chain | Residue | Details |
| A | SER245 | |
| B | SER245 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1nf9 |
| Chain | Residue | Details |
| A | ASP37 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1nf9 |
| Chain | Residue | Details |
| B | ASP37 |
