2BPQ
Anthranilate phosphoribosyltransferase (TrpD) from Mycobacterium tuberculosis (Apo structure)
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 | 8 |
| Details | BINDING SITE FOR RESIDUE BEN A 1369 |
| Chain | Residue |
| A | THR70 |
| A | MET71 |
| A | LYS72 |
| A | ASP225 |
| A | HOH2140 |
| B | THR35 |
| B | ASN37 |
| B | GOL1376 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE BEN B 1374 |
| Chain | Residue |
| B | MET69 |
| B | THR70 |
| B | MET71 |
| B | LYS72 |
| B | ASP225 |
| A | ASN37 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE BEN B 1375 |
| Chain | Residue |
| B | GLY80 |
| B | THR353 |
| B | ALA355 |
| B | HOH2018 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL A 1370 |
| Chain | Residue |
| A | PHE274 |
| A | ASP275 |
| A | GLY278 |
| A | PHE279 |
| A | TRP336 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL B 1376 |
| Chain | Residue |
| A | THR70 |
| A | PRO199 |
| A | BEN1369 |
| A | HOH2073 |
| B | THR35 |
| B | ASP36 |
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 | 25 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| 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 |
