2GVQ
Anthranilate phosphoribosyl-transferase (TRPD) from S. solfataricus in complex with anthranilate
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 | 0005829 | cellular_component | cytosol |
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 | 0005829 | cellular_component | cytosol |
B | 0016757 | molecular_function | glycosyltransferase activity |
B | 0016763 | molecular_function | pentosyltransferase activity |
B | 0046872 | molecular_function | metal ion binding |
C | 0000162 | biological_process | tryptophan biosynthetic process |
C | 0000287 | molecular_function | magnesium ion binding |
C | 0004048 | molecular_function | anthranilate phosphoribosyltransferase activity |
C | 0005829 | cellular_component | cytosol |
C | 0016757 | molecular_function | glycosyltransferase activity |
C | 0016763 | molecular_function | pentosyltransferase activity |
C | 0046872 | molecular_function | metal ion binding |
D | 0000162 | biological_process | tryptophan biosynthetic process |
D | 0000287 | molecular_function | magnesium ion binding |
D | 0004048 | molecular_function | anthranilate phosphoribosyltransferase activity |
D | 0005829 | cellular_component | cytosol |
D | 0016757 | molecular_function | glycosyltransferase activity |
D | 0016763 | molecular_function | pentosyltransferase activity |
D | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE BE2 A 346 |
Chain | Residue |
A | ASN109 |
A | ALA150 |
A | GLN151 |
A | HIS154 |
A | ARG164 |
A | GLY177 |
site_id | AC2 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE BE2 B 401 |
Chain | Residue |
B | MET157 |
B | ARG164 |
B | PHE173 |
B | BE2402 |
B | ASN109 |
B | GLN151 |
B | HIS154 |
site_id | AC3 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE BE2 B 402 |
Chain | Residue |
B | GLY79 |
B | THR80 |
B | HIS107 |
B | ASN109 |
B | ALA150 |
B | GLY177 |
B | PRO178 |
B | BE2401 |
site_id | AC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE BE2 C 501 |
Chain | Residue |
C | HIS107 |
C | ASN109 |
C | GLY177 |
C | BE2502 |
site_id | AC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE BE2 C 502 |
Chain | Residue |
C | ASN109 |
C | HIS154 |
C | MET157 |
C | ARG164 |
C | BE2501 |
site_id | AC6 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE BE2 D 601 |
Chain | Residue |
D | GLY79 |
D | THR80 |
D | HIS107 |
D | ASN109 |
D | GLY177 |
D | PRO178 |
D | BE2602 |
site_id | AC7 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE BE2 D 602 |
Chain | Residue |
D | ASN109 |
D | ALA150 |
D | GLN151 |
D | HIS154 |
D | MET157 |
D | ARG164 |
D | BE2601 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 40 |
Details | BINDING: |
Chain | Residue | Details |
A | THR77 | |
A | GLU224 | |
B | THR77 | |
B | GLY79 | |
B | GLY82 | |
B | ASN89 | |
B | SER91 | |
B | LYS106 | |
B | ASN109 | |
B | ARG164 | |
B | ASP223 | |
A | GLY79 | |
B | GLU224 | |
C | THR77 | |
C | GLY79 | |
C | GLY82 | |
C | ASN89 | |
C | SER91 | |
C | LYS106 | |
C | ASN109 | |
C | ARG164 | |
C | ASP223 | |
A | GLY82 | |
C | GLU224 | |
D | THR77 | |
D | GLY79 | |
D | GLY82 | |
D | ASN89 | |
D | SER91 | |
D | LYS106 | |
D | ASN109 | |
D | ARG164 | |
D | ASP223 | |
A | ASN89 | |
D | GLU224 | |
A | SER91 | |
A | LYS106 | |
A | ASN109 | |
A | ARG164 | |
A | ASP223 |
site_id | SWS_FT_FI2 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00211, ECO:0000269|PubMed:16714288, ECO:0000269|PubMed:19385665 |
Chain | Residue | Details |
A | THR87 | |
A | SER118 | |
B | THR87 | |
B | SER118 | |
C | THR87 | |
C | SER118 | |
D | THR87 | |
D | SER118 |