2GVQ
Anthranilate phosphoribosyl-transferase (TRPD) from S. solfataricus in complex with anthranilate
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 |
| C | 0000162 | biological_process | L-tryptophan biosynthetic process |
| C | 0000287 | molecular_function | magnesium ion binding |
| C | 0004048 | molecular_function | anthranilate phosphoribosyltransferase activity |
| C | 0005829 | cellular_component | cytosol |
| C | 0016757 | molecular_function | glycosyltransferase activity |
| C | 0016763 | molecular_function | pentosyltransferase activity |
| D | 0000162 | biological_process | L-tryptophan biosynthetic process |
| D | 0000287 | molecular_function | magnesium ion binding |
| D | 0004048 | molecular_function | anthranilate phosphoribosyltransferase activity |
| D | 0005829 | cellular_component | cytosol |
| D | 0016757 | molecular_function | glycosyltransferase activity |
| D | 0016763 | molecular_function | pentosyltransferase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE BE2 A 346 |
| Chain | Residue |
| A | ASN109 |
| A | ALA150 |
| A | GLN151 |
| A | HIS154 |
| A | ARG164 |
| A | GLY177 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE BE2 B 401 |
| Chain | Residue |
| B | MET157 |
| B | ARG164 |
| B | PHE173 |
| B | BE2402 |
| B | ASN109 |
| B | GLN151 |
| B | HIS154 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE BE2 B 402 |
| Chain | Residue |
| B | GLY79 |
| B | THR80 |
| B | HIS107 |
| B | ASN109 |
| B | ALA150 |
| B | GLY177 |
| B | PRO178 |
| B | BE2401 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE BE2 C 501 |
| Chain | Residue |
| C | HIS107 |
| C | ASN109 |
| C | GLY177 |
| C | BE2502 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE BE2 C 502 |
| Chain | Residue |
| C | ASN109 |
| C | HIS154 |
| C | MET157 |
| C | ARG164 |
| C | BE2501 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE BE2 D 601 |
| Chain | Residue |
| D | GLY79 |
| D | THR80 |
| D | HIS107 |
| D | ASN109 |
| D | GLY177 |
| D | PRO178 |
| D | BE2602 |
| site_id | AC7 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE BE2 D 602 |
| Chain | Residue |
| D | ASN109 |
| D | ALA150 |
| D | GLN151 |
| D | HIS154 |
| D | MET157 |
| D | ARG164 |
| D | BE2601 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 77 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00211","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"16714288","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19385665","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
