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 | 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 | 0016757 | molecular_function | glycosyltransferase activity |
A | 0016763 | molecular_function | pentosyltransferase activity |
A | 0046872 | molecular_function | metal ion binding |
B | 0000162 | biological_process | 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 | 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: BINDING => ECO:0000255|HAMAP-Rule:MF_00211 |
Chain | Residue | Details |
A | VAL106 | |
B | VAL106 |
site_id | SWS_FT_FI2 |
Number of Residues | 16 |
Details | BINDING: |
Chain | Residue | Details |
A | GLY109 | |
B | VAL116 | |
B | LEU118 | |
B | VAL134 | |
B | GLY137 | |
B | VAL192 | |
B | LEU250 | |
B | ASP251 | |
A | VAL116 | |
A | LEU118 | |
A | VAL134 | |
A | GLY137 | |
A | VAL192 | |
A | LEU250 | |
A | ASP251 | |
B | GLY109 |
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 | ASN114 | |
A | GLY146 | |
B | ASN114 | |
B | GLY146 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | MOD_RES: N-acetylalanine => ECO:0007744|PubMed:21969609 |
Chain | Residue | Details |
A | VAL1 | |
B | VAL1 |