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 | Active site: {"description":"Proton donor","evidences":[{"source":"HAMAP-Rule","id":"MF_01930","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10433709","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 10 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01930","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10606510","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"1631098","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01930","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10606510","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 14 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"10606510","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"1631098","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Site: {"description":"Raises pKa of active site His","evidences":[{"source":"HAMAP-Rule","id":"MF_01930","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10433709","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
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 |
