1VQU
Crystal structure of Anthranilate phosphoribosyltransferase 2 (17130499) from Nostoc sp. at 1.85 A resolution
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000162 | biological_process | L-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 |
| B | 0000162 | biological_process | L-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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ACT A 363 |
| Chain | Residue |
| A | ASN113 |
| A | ILE114 |
| A | SER115 |
| A | THR116 |
| A | HOH494 |
| site_id | AC2 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE GOL B 363 |
| Chain | Residue |
| B | GLY105 |
| B | SER136 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 40 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00211","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
