Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003824 | molecular_function | catalytic activity |
A | 0009058 | biological_process | biosynthetic process |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE BME A 311 |
Chain | Residue |
A | TYR105 |
A | HIS106 |
A | GLY115 |
A | ASP142 |
site_id | AC2 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE BME A 312 |
Chain | Residue |
A | LEU147 |
A | PRO189 |
A | CYS191 |
site_id | AC3 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE BME A 313 |
Chain | Residue |
A | LYS307 |
A | CYS238 |
A | PHE305 |
site_id | AC4 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE BME A 314 |
Chain | Residue |
A | CYS152 |
A | GLU153 |
A | ARG166 |
site_id | AC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE BME A 315 |
Chain | Residue |
A | THR31 |
A | PHE56 |
A | TRP59 |
A | CYS86 |
A | GLN88 |
Functional Information from PROSITE/UniProt
site_id | PS00373 |
Number of Residues | 24 |
Details | GART Phosphoribosylglycinamide formyltransferase active site. GfTIfWAdDgLDtGdlLlqkeceV |
Chain | Residue | Details |
A | GLY131-VAL154 | |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | HIS106 | |
Chain | Residue | Details |
A | GLN88 | |
A | ASP142 | |
Chain | Residue | Details |
A | ASP142 | |
Chain | Residue | Details |
A | LYS38 | |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 1 |
Details | a catalytic site defined by CSA, PubMed 14729668, 10585460, 11320079 |
Chain | Residue | Details |
A | ASP142 | |
site_id | MCSA1 |
Number of Residues | 2 |
Details | M-CSA 766 |
Chain | Residue | Details |
A | HIS106 | electrostatic stabiliser |
A | ASP142 | electrostatic stabiliser |