1JVN
CRYSTAL STRUCTURE OF IMIDAZOLE GLYCEROL PHOSPHATE SYNTHASE: A TUNNEL THROUGH A (BETA/ALPHA)8 BARREL JOINS TWO ACTIVE SITES
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000105 | biological_process | L-histidine biosynthetic process |
A | 0000107 | molecular_function | imidazoleglycerol-phosphate synthase activity |
A | 0004359 | molecular_function | glutaminase activity |
A | 0005737 | cellular_component | cytoplasm |
A | 0006541 | biological_process | glutamine metabolic process |
A | 0008652 | biological_process | amino acid biosynthetic process |
A | 0016763 | molecular_function | pentosyltransferase activity |
A | 0016787 | molecular_function | hydrolase activity |
A | 0016829 | molecular_function | lyase activity |
A | 0016833 | molecular_function | oxo-acid-lyase activity |
A | 0044281 | biological_process | small molecule metabolic process |
B | 0000105 | biological_process | L-histidine biosynthetic process |
B | 0000107 | molecular_function | imidazoleglycerol-phosphate synthase activity |
B | 0004359 | molecular_function | glutaminase activity |
B | 0005737 | cellular_component | cytoplasm |
B | 0006541 | biological_process | glutamine metabolic process |
B | 0008652 | biological_process | amino acid biosynthetic process |
B | 0016763 | molecular_function | pentosyltransferase activity |
B | 0016787 | molecular_function | hydrolase activity |
B | 0016829 | molecular_function | lyase activity |
B | 0016833 | molecular_function | oxo-acid-lyase activity |
B | 0044281 | biological_process | small molecule metabolic process |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE NI B 901 |
Chain | Residue |
B | HIS-1 |
B | SER-2 |
B | GLY-3 |
B | MET1 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE NI A 902 |
Chain | Residue |
A | HIS-1 |
A | GLY-3 |
A | SER-2 |
A | MET1 |
B | TYR425 |
site_id | AC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 A 801 |
Chain | Residue |
A | GLY331 |
A | GLY364 |
A | THR365 |
A | HOH1010 |
site_id | AC4 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE SO4 A 802 |
Chain | Residue |
A | GLY475 |
A | ASN477 |
A | GLY524 |
A | ARG528 |
A | HOH974 |
A | HOH1073 |
A | HOH1103 |
site_id | AC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 B 803 |
Chain | Residue |
B | LYS158 |
B | LYS170 |
B | LYS343 |
B | HOH1136 |
site_id | AC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 B 804 |
Chain | Residue |
B | GLY331 |
B | GLY364 |
B | THR365 |
B | HOH1012 |
B | HOH1132 |
B | HOH1172 |
site_id | AC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 A 806 |
Chain | Residue |
A | SER130 |
A | GLU131 |
A | ASN132 |
B | LYS493 |
site_id | AC8 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE POP B 999 |
Chain | Residue |
B | ASP474 |
B | GLY475 |
B | ASN477 |
B | GLY501 |
B | GLY524 |
B | MET525 |
B | ARG528 |
B | HOH1013 |
B | HOH1052 |
B | HOH1113 |
Functional Information from PROSITE/UniProt
site_id | PS00599 |
Number of Residues | 10 |
Details | AA_TRANSFER_CLASS_2 Aminotransferases class-II pyridoxal-phosphate attachment site. TISKAYGAQA |
Chain | Residue | Details |
A | THR389-ALA398 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 6 |
Details | ACT_SITE: For GATase activity => ECO:0000250 |
Chain | Residue | Details |
A | 14383 | |
A | HIS193 | |
A | GLU195 | |
B | 14383 | |
B | HIS193 | |
B | GLU195 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | ACT_SITE: ACT_SITE => ECO:0000255 |
Chain | Residue | Details |
A | ASP245 | |
A | ASP404 | |
B | ASP245 | |
B | ASP404 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | BINDING: covalent |
Chain | Residue | Details |
A | 14383 | |
B | 14383 |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | BINDING: |
Chain | Residue | Details |
A | GLY332 | |
A | ASN469 | |
B | GLY332 | |
B | ASN469 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1bxr |
Chain | Residue | Details |
A | GLU195 | |
A | 14383 | |
A | HIS193 |
site_id | CSA2 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1bxr |
Chain | Residue | Details |
B | GLU195 | |
B | 14383 | |
B | HIS193 |
site_id | CSA3 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1bxr |
Chain | Residue | Details |
A | ASP245 | |
A | ASP404 |
site_id | CSA4 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1bxr |
Chain | Residue | Details |
B | ASP245 | |
B | ASP404 |
site_id | CSA5 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1bxr |
Chain | Residue | Details |
A | HIS193 |
site_id | CSA6 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1bxr |
Chain | Residue | Details |
B | HIS193 |