4IJ1
Bianthranilate-like analogue bound to anthranilate phosphoribosyltransferase (AnPRT; trpD) in absence of substrates.
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 | 0005576 | cellular_component | extracellular region |
| A | 0005829 | cellular_component | cytosol |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0008652 | biological_process | amino acid biosynthetic process |
| A | 0009073 | biological_process | aromatic amino acid family biosynthetic process |
| A | 0016740 | molecular_function | transferase activity |
| A | 0016757 | molecular_function | glycosyltransferase activity |
| A | 0016763 | molecular_function | pentosyltransferase activity |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0000162 | biological_process | L-tryptophan biosynthetic process |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0004048 | molecular_function | anthranilate phosphoribosyltransferase activity |
| B | 0005576 | cellular_component | extracellular region |
| B | 0005829 | cellular_component | cytosol |
| B | 0005886 | cellular_component | plasma membrane |
| B | 0008652 | biological_process | amino acid biosynthetic process |
| B | 0009073 | biological_process | aromatic amino acid family biosynthetic process |
| B | 0016740 | molecular_function | transferase activity |
| 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 | 13 |
| Details | BINDING SITE FOR RESIDUE 17C A 401 |
| Chain | Residue |
| A | MET86 |
| A | ARG194 |
| A | GOL402 |
| A | HOH533 |
| A | HOH696 |
| A | ASN138 |
| A | ALA179 |
| A | PRO180 |
| A | HIS183 |
| A | TYR186 |
| A | ARG187 |
| A | ALA190 |
| A | ARG193 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL A 402 |
| Chain | Residue |
| A | GLY107 |
| A | GLY206 |
| A | PRO207 |
| A | 17C401 |
| A | HOH697 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE IMD A 403 |
| Chain | Residue |
| A | ARG237 |
| A | LEU305 |
| A | GLY306 |
| A | GLY307 |
| A | ILE351 |
| A | GLU357 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE IMD A 404 |
| Chain | Residue |
| A | TRP47 |
| A | ASP50 |
| A | GLU342 |
| A | ARG346 |
| site_id | AC5 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE 17C B 401 |
| Chain | Residue |
| B | HIS91 |
| B | ASN138 |
| B | PRO180 |
| B | PRO180 |
| B | ARG181 |
| B | HIS183 |
| B | TYR186 |
| B | ARG187 |
| B | ALA190 |
| B | ARG194 |
| B | GOL403 |
| B | HOH536 |
| B | HOH679 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL B 402 |
| Chain | Residue |
| B | ALA46 |
| B | TRP47 |
| B | ASP50 |
| B | GLU342 |
| B | ARG346 |
| B | HOH539 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL B 403 |
| Chain | Residue |
| B | HIS91 |
| B | PRO162 |
| B | ARG181 |
| B | ARG194 |
| B | 17C401 |
| site_id | AC8 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE GOL B 404 |
| Chain | Residue |
| B | ALA236 |
| B | ARG237 |
| B | ARG238 |
| B | LEU305 |
| B | GLY306 |
| B | GLY307 |
| B | ILE351 |
| B | ASP352 |
| B | GLU357 |
| B | HOH592 |
| B | HOH663 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00211","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00211","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"16337227","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23363292","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"FEB-2011","submissionDatabase":"PDB data bank","title":"Inhibition of Mycobacterium tuberculosis anthranilate phosphoribosyltransferase by blocking of an active site entrance tunnel.","authors":["Castell A.","Short L.F.","Evans G.","Bulloch E.M.","Cookson T.","Parker E.","Lee C.","Baker E.N.","Lott J.S."]}},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"AUG-2012","submissionDatabase":"PDB data bank","title":"Improved inhibitors against Mycobacterium tuberculosis anthranilate phosphoribosyltransferase.","authors":["Evans G.L.","Gamage S.A.","Denny W.A.","Baker E.N.","Lott J.S."]}}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 16 |
| Details | Binding site: {} |
| Chain | Residue | Details |
