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: BINDING => ECO:0000255|HAMAP-Rule:MF_00211 |
Chain | Residue | Details |
A | GLY107 | |
B | GLY107 |
site_id | SWS_FT_FI2 |
Number of Residues | 16 |
Details | BINDING: |
Chain | Residue | Details |
A | GLY110 | |
B | ASN117 | |
B | SER119 | |
B | LYS135 | |
B | ASN138 | |
B | ARG193 | |
B | ASP251 | |
B | GLU252 | |
A | ASN117 | |
A | SER119 | |
A | LYS135 | |
A | ASN138 | |
A | ARG193 | |
A | ASP251 | |
A | GLU252 | |
B | GLY110 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00211, ECO:0000269|PubMed:16337227, ECO:0000269|PubMed:23363292, ECO:0000269|Ref.4, ECO:0000269|Ref.5 |
Chain | Residue | Details |
A | THR115 | |
A | GLY147 | |
B | THR115 | |
B | GLY147 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | MOD_RES: N-acetylalanine => ECO:0007744|PubMed:21969609 |
Chain | Residue | Details |
A | ALA2 | |
B | ALA2 |