1C3E
NEW INSIGHTS INTO INHIBITOR DESIGN FROM THE CRYSTAL STRUCTURE AND NMR STUDIES OF E. COLI GAR TRANSFORMYLATE IN COMPLEX WITH BETA-GAR AND 10-FORMYL-5,8,10-TRIDEAZAFOLIC ACID.
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003824 | molecular_function | catalytic activity |
A | 0004644 | molecular_function | phosphoribosylglycinamide formyltransferase activity |
A | 0005737 | cellular_component | cytoplasm |
A | 0005829 | cellular_component | cytosol |
A | 0006164 | biological_process | purine nucleotide biosynthetic process |
A | 0006189 | biological_process | 'de novo' IMP biosynthetic process |
A | 0006974 | biological_process | DNA damage response |
A | 0009058 | biological_process | biosynthetic process |
A | 0016740 | molecular_function | transferase activity |
B | 0003824 | molecular_function | catalytic activity |
B | 0004644 | molecular_function | phosphoribosylglycinamide formyltransferase activity |
B | 0005737 | cellular_component | cytoplasm |
B | 0005829 | cellular_component | cytosol |
B | 0006164 | biological_process | purine nucleotide biosynthetic process |
B | 0006189 | biological_process | 'de novo' IMP biosynthetic process |
B | 0006974 | biological_process | DNA damage response |
B | 0009058 | biological_process | biosynthetic process |
B | 0016740 | molecular_function | transferase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE NHR A 220 |
Chain | Residue |
A | ARG64 |
A | LEU118 |
A | VAL139 |
A | THR140 |
A | GLU142 |
A | LEU143 |
A | ASP144 |
A | GAR221 |
A | PHE88 |
A | MET89 |
A | ARG90 |
A | ILE91 |
A | LEU92 |
A | VAL97 |
A | ASN106 |
A | HIS108 |
site_id | AC2 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE GAR A 221 |
Chain | Residue |
A | GLY11 |
A | SER12 |
A | ASN13 |
A | GLY87 |
A | PHE88 |
A | MET89 |
A | ILE107 |
A | PRO109 |
A | GLU173 |
A | NHR220 |
A | HOH225 |
A | HOH232 |
A | HOH269 |
site_id | AC3 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE NHR B 222 |
Chain | Residue |
A | GLU131 |
B | ARG64 |
B | PHE88 |
B | MET89 |
B | ARG90 |
B | ILE91 |
B | LEU92 |
B | VAL97 |
B | ASN106 |
B | HIS108 |
B | LEU118 |
B | VAL139 |
B | THR140 |
B | GLU142 |
B | ASP144 |
B | GAR223 |
site_id | AC4 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE GAR B 223 |
Chain | Residue |
B | ASN10 |
B | GLY11 |
B | SER12 |
B | ASN13 |
B | GLY87 |
B | PHE88 |
B | MET89 |
B | ILE107 |
B | PRO109 |
B | GLU173 |
B | NHR222 |
B | HOH246 |
B | HOH248 |
B | HOH289 |
B | HOH291 |
Functional Information from PROSITE/UniProt
site_id | PS00373 |
Number of Residues | 24 |
Details | GART Phosphoribosylglycinamide formyltransferase active site. GtSVhFVtDeLDgGpvIlqakvpV |
Chain | Residue | Details |
A | GLY133-VAL156 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | ACT_SITE: Proton donor => ECO:0000255|HAMAP-Rule:MF_01930, ECO:0000269|PubMed:10433709 |
Chain | Residue | Details |
A | HIS108 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01930, ECO:0000269|PubMed:10606510, ECO:0000269|PubMed:1631098 |
Chain | Residue | Details |
A | GLY11 | |
A | MET89 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01930, ECO:0000269|PubMed:10606510 |
Chain | Residue | Details |
A | ARG64 | |
A | ASN106 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:10606510, ECO:0000269|PubMed:1631098 |
Chain | Residue | Details |
A | THR140 | |
A | GLN170 |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | SITE: Raises pKa of active site His => ECO:0000255|HAMAP-Rule:MF_01930, ECO:0000269|PubMed:10433709 |
Chain | Residue | Details |
A | ASP144 |
Catalytic Information from CSA
site_id | MCSA1 |
Number of Residues | 4 |
Details | M-CSA 363 |
Chain | Residue | Details |
A | ASN106 | electrostatic stabiliser, hydrogen bond donor, increase electrophilicity |
A | HIS108 | activator, attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor, increase electrophilicity |
A | SER135 | electrostatic stabiliser, hydrogen bond donor, steric role |
A | ASP144 | attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond acceptor, increase electrophilicity |