4X5D
Anthranilate phosphoribosyltransferase variant R193A from Mycobacterium tuberculosis with anthranilate bound
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 BE2 A 401 |
Chain | Residue |
A | ASN138 |
A | ALA179 |
A | PRO180 |
A | HIS183 |
A | TYR186 |
A | ALA190 |
A | ARG194 |
A | HOH591 |
site_id | AC2 |
Number of Residues | 5 |
Details | binding site for residue IMD A 402 |
Chain | Residue |
A | GLY306 |
A | ILE351 |
A | ASP352 |
A | GLU357 |
A | LEU305 |
site_id | AC3 |
Number of Residues | 5 |
Details | binding site for residue GOL A 403 |
Chain | Residue |
A | THR273 |
A | PHE274 |
A | ASP275 |
A | GLY278 |
A | TRP336 |
site_id | AC4 |
Number of Residues | 7 |
Details | binding site for residue BE2 B 401 |
Chain | Residue |
B | ASN138 |
B | HIS183 |
B | TYR186 |
B | ARG187 |
B | ALA190 |
B | ARG194 |
B | HOH553 |
site_id | AC5 |
Number of Residues | 6 |
Details | binding site for residue GOL B 402 |
Chain | Residue |
B | PHE274 |
B | ASP275 |
B | PHE279 |
B | TRP336 |
B | HOH509 |
B | HOH520 |
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 |