4HKM
Crystal Structure of an Anthranilate Phosphoribosyltransferase (target ID NYSGRC-016600) from Xanthomonas campestris
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000162 | biological_process | tryptophan biosynthetic process |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0004048 | molecular_function | anthranilate phosphoribosyltransferase activity |
| A | 0005829 | cellular_component | cytosol |
| A | 0016757 | molecular_function | glycosyltransferase activity |
| A | 0016763 | molecular_function | pentosyltransferase activity |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0000162 | biological_process | tryptophan biosynthetic process |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0004048 | molecular_function | anthranilate phosphoribosyltransferase activity |
| B | 0005829 | cellular_component | cytosol |
| B | 0016757 | molecular_function | glycosyltransferase activity |
| B | 0016763 | molecular_function | pentosyltransferase activity |
| B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PO4 A 401 |
| Chain | Residue |
| A | SER68 |
| A | ARG69 |
| A | ARG70 |
| A | HOH614 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE PO4 A 402 |
| Chain | Residue |
| A | ARG317 |
| A | HOH607 |
| B | VAL316 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL A 403 |
| Chain | Residue |
| A | ARG176 |
| A | THR177 |
| A | ILE178 |
| A | ASN180 |
| A | ILE181 |
| A | ARG48 |
| A | GLU52 |
| site_id | AC4 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE CXS B 401 |
| Chain | Residue |
| B | GLU241 |
| B | TYR250 |
| B | PHE257 |
| B | TYR303 |
| B | SER310 |
| B | ILE311 |
| B | HOH513 |
| B | HOH566 |
| B | HOH582 |
| site_id | AC5 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE PO4 B 402 |
| Chain | Residue |
| A | GLU17 |
| A | THR53 |
| A | ILE54 |
| A | GLY55 |
| B | GLU17 |
| B | THR53 |
| B | ILE54 |
| B | GLY55 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PO4 B 403 |
| Chain | Residue |
| B | ARG48 |
| B | GLU52 |
| B | ARG176 |
| B | THR177 |
| B | ILE178 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PO4 B 404 |
| Chain | Residue |
| B | ASN94 |
| B | SER96 |
| B | THR97 |
| B | LYS112 |
| site_id | AC8 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE PO4 B 405 |
| Chain | Residue |
| B | ARG170 |
| site_id | AC9 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL B 406 |
| Chain | Residue |
| B | GLU66 |
| B | PHE67 |
| B | HOH567 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 18 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00211 |
| Chain | Residue | Details |
| A | GLY84 | |
| B | GLY84 | |
| B | GLY87 | |
| B | THR92 | |
| B | SER96 | |
| B | ASN115 | |
| B | SER124 | |
| B | ARG170 | |
| B | ASP229 | |
| B | GLU230 | |
| A | GLY87 | |
| A | THR92 | |
| A | SER96 | |
| A | ASN115 | |
| A | SER124 | |
| A | ARG170 | |
| A | ASP229 | |
| A | GLU230 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | ASN94 | |
| A | LYS112 | |
| B | ASN94 | |
| B | LYS112 |
