4X5E
Anthranilate phosphoribosyltransferase variant R194A from Mycobacterium tuberculosis with pyrophosphate, Mg2+ and 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 | 17 |
| Details | binding site for residue POP A 401 |
| Chain | Residue |
| A | VAL106 |
| A | MG402 |
| A | MG403 |
| A | HOH594 |
| A | HOH652 |
| A | HOH653 |
| A | HOH713 |
| A | HOH714 |
| A | HOH727 |
| A | GLY107 |
| A | ASN117 |
| A | LEU118 |
| A | SER119 |
| A | THR120 |
| A | LYS135 |
| A | GLY147 |
| A | GLU252 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue MG A 402 |
| Chain | Residue |
| A | SER119 |
| A | GLU252 |
| A | POP401 |
| A | MG403 |
| A | HOH586 |
| A | HOH594 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | binding site for residue MG A 403 |
| Chain | Residue |
| A | ASP251 |
| A | GLU252 |
| A | POP401 |
| A | MG402 |
| A | HOH594 |
| A | HOH598 |
| A | HOH612 |
| A | HOH652 |
| site_id | AC4 |
| Number of Residues | 10 |
| Details | binding site for residue BE2 A 404 |
| Chain | Residue |
| A | VAL106 |
| A | GLY107 |
| A | THR108 |
| A | HIS136 |
| A | ASN138 |
| A | ARG193 |
| A | GLY206 |
| A | BE2405 |
| A | HOH638 |
| A | HOH755 |
| site_id | AC5 |
| Number of Residues | 11 |
| Details | binding site for residue BE2 A 405 |
| Chain | Residue |
| A | MET86 |
| A | ASN138 |
| A | ALA179 |
| A | PRO180 |
| A | TYR186 |
| A | ARG193 |
| A | GLY206 |
| A | BE2404 |
| A | HOH626 |
| A | HOH639 |
| A | HOH670 |
| site_id | AC6 |
| Number of Residues | 12 |
| Details | binding site for residue GOL A 406 |
| Chain | Residue |
| A | ARG215 |
| A | ALA236 |
| A | ARG237 |
| A | ARG238 |
| A | LEU305 |
| A | GLY306 |
| A | GLY307 |
| A | ILE351 |
| A | ASP352 |
| A | GLU357 |
| A | HOH522 |
| A | HOH817 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | binding site for residue GOL A 407 |
| Chain | Residue |
| A | GLY43 |
| A | ALA46 |
| A | TRP47 |
| A | ASP50 |
| A | ARG346 |
| A | HOH530 |
| site_id | AC8 |
| Number of Residues | 11 |
| Details | binding site for residue POP B 401 |
| Chain | Residue |
| B | VAL106 |
| B | GLY107 |
| B | ASN117 |
| B | SER119 |
| B | THR120 |
| B | LYS135 |
| B | GLU252 |
| B | MG402 |
| B | MG403 |
| B | HOH593 |
| B | HOH682 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | binding site for residue MG B 402 |
| Chain | Residue |
| B | SER119 |
| B | GLU252 |
| B | POP401 |
| B | MG403 |
| B | HOH586 |
| B | HOH682 |
| site_id | AD1 |
| Number of Residues | 7 |
| Details | binding site for residue MG B 403 |
| Chain | Residue |
| B | THR115 |
| B | ASP251 |
| B | GLU252 |
| B | POP401 |
| B | MG402 |
| B | HOH622 |
| B | HOH682 |
| site_id | AD2 |
| Number of Residues | 6 |
| Details | binding site for residue BE2 B 404 |
| Chain | Residue |
| B | ALA190 |
| B | ASN138 |
| B | PRO180 |
| B | HIS183 |
| B | TYR186 |
| B | ARG187 |
| site_id | AD3 |
| Number of Residues | 7 |
| Details | binding site for residue BE2 B 405 |
| Chain | Residue |
| B | GLY137 |
| B | ASN138 |
| B | GLY206 |
| B | HOH637 |
| B | HOH649 |
| B | HOH660 |
| B | HOH673 |
| site_id | AD4 |
| Number of Residues | 6 |
| Details | binding site for residue GOL B 406 |
| Chain | Residue |
| B | GLY43 |
| B | ALA46 |
| B | TRP47 |
| B | ASP50 |
| B | GLU342 |
| B | ARG346 |
| site_id | AD5 |
| Number of Residues | 8 |
| Details | binding site for residue GOL B 407 |
| Chain | Residue |
| B | ARG237 |
| B | ARG238 |
| B | LEU305 |
| B | GLY306 |
| B | GLY307 |
| B | ILE351 |
| B | ASP352 |
| B | GLU357 |
| site_id | AD6 |
| Number of Residues | 2 |
| Details | binding site for residue GOL B 408 |
| Chain | Residue |
| B | ARG263 |
| B | VAL325 |
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 | 18 |
| 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 |
