1CDD
STRUCTURES OF APO AND COMPLEXED ESCHERICHIA COLI GLYCINAMIDE RIBONUCLEOTIDE TRANSFORMYLASE
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 | 6 |
Details | BINDING SITE FOR RESIDUE PO4 A 221 |
Chain | Residue |
A | ASN10 |
A | GLY11 |
A | SER12 |
A | ASN13 |
A | ALA86 |
B | GLU212 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE PO4 B 221 |
Chain | Residue |
B | ASN13 |
B | GLN170 |
B | ASN10 |
B | GLY11 |
B | SER12 |
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 | CSA1 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1c2t |
Chain | Residue | Details |
A | SER135 | |
A | ASN106 | |
A | ASP144 | |
A | HIS108 |
site_id | CSA2 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1c2t |
Chain | Residue | Details |
B | SER135 | |
B | ASN106 | |
B | ASP144 | |
B | HIS108 |
site_id | CSA3 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1c2t |
Chain | Residue | Details |
A | ASN106 | |
A | ASP144 | |
A | HIS108 |
site_id | CSA4 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1c2t |
Chain | Residue | Details |
B | ASN106 | |
B | ASP144 | |
B | HIS108 |
site_id | CSA5 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1c2t |
Chain | Residue | Details |
A | ASP144 | |
A | HIS108 |
site_id | CSA6 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1c2t |
Chain | Residue | Details |
B | ASP144 | |
B | HIS108 |
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 |