1GRC
CRYSTAL STRUCTURE OF GLYCINAMIDE RIBONUCLEOTIDE TRANSFORMYLASE FROM ESCHERICHIA COLI AT 3.0 ANGSTROMS RESOLUTION: A TARGET ENZYME FOR CHEMOTHERAPY
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 | 5 |
| Details | BINDING SITE FOR RESIDUE PO4 A 301 |
| Chain | Residue |
| A | ASN10 |
| A | GLY11 |
| A | SER12 |
| A | ASN13 |
| A | ALA86 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PO4 B 301 |
| Chain | Residue |
| B | GLY11 |
| B | SER12 |
| B | ASN13 |
| B | GLN170 |
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 | 2 |
| Details | ACT_SITE: Proton donor => ECO:0000255|HAMAP-Rule:MF_01930, ECO:0000269|PubMed:10433709 |
| Chain | Residue | Details |
| A | HIS108 | |
| B | HIS108 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01930, ECO:0000269|PubMed:10606510, ECO:0000269|PubMed:1631098 |
| Chain | Residue | Details |
| A | GLY11 | |
| A | MET89 | |
| B | GLY11 | |
| B | MET89 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01930, ECO:0000269|PubMed:10606510 |
| Chain | Residue | Details |
| A | ARG64 | |
| A | ASN106 | |
| B | ARG64 | |
| B | ASN106 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:10606510, ECO:0000269|PubMed:1631098 |
| Chain | Residue | Details |
| A | THR140 | |
| A | GLN170 | |
| B | THR140 | |
| B | GLN170 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | SITE: Raises pKa of active site His => ECO:0000255|HAMAP-Rule:MF_01930, ECO:0000269|PubMed:10433709 |
| Chain | Residue | Details |
| A | ASP144 | |
| B | 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 |
| site_id | MCSA2 |
| Number of Residues | 4 |
| Details | M-CSA 363 |
| Chain | Residue | Details |
| B | ASN106 | electrostatic stabiliser, hydrogen bond donor, increase electrophilicity |
| B | HIS108 | activator, attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor, increase electrophilicity |
| B | SER135 | electrostatic stabiliser, hydrogen bond donor, steric role |
| B | ASP144 | attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond acceptor, increase electrophilicity |
