1RC0
Human GAR Tfase complex structure with polyglutamated 10-(trifluoroacetyl)-5,10-dideazaacyclic-5,6,7,8-tetrahydrofolic acid
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004644 | molecular_function | phosphoribosylglycinamide formyltransferase activity |
A | 0006189 | biological_process | 'de novo' IMP biosynthetic process |
A | 0009058 | biological_process | biosynthetic process |
B | 0004644 | molecular_function | phosphoribosylglycinamide formyltransferase activity |
B | 0006189 | biological_process | 'de novo' IMP biosynthetic process |
B | 0009058 | biological_process | biosynthetic process |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE KT5 A 510 |
Chain | Residue |
A | ARG64 |
A | SER118 |
A | VAL139 |
A | ALA140 |
A | GLU141 |
A | VAL143 |
A | ASP144 |
A | HOH538 |
A | HOH572 |
A | MET89 |
A | ARG90 |
A | ILE91 |
A | LEU92 |
A | ASN106 |
A | HIS108 |
A | PRO109 |
A | GLY117 |
site_id | AC2 |
Number of Residues | 23 |
Details | BINDING SITE FOR RESIDUE KT5 B 610 |
Chain | Residue |
B | ARG64 |
B | MET89 |
B | ARG90 |
B | ILE91 |
B | LEU92 |
B | VAL97 |
B | ASN106 |
B | HIS108 |
B | PRO109 |
B | GLY117 |
B | SER118 |
B | VAL139 |
B | ALA140 |
B | GLU141 |
B | VAL143 |
B | ASP144 |
B | HOH613 |
B | HOH620 |
B | HOH641 |
B | HOH657 |
B | HOH666 |
B | HOH684 |
B | HOH702 |
Functional Information from PROSITE/UniProt
site_id | PS00373 |
Number of Residues | 24 |
Details | GART Phosphoribosylglycinamide formyltransferase active site. GcTVhFVaEdVDaGqiIlqeavpV |
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":"UniProtKB","id":"P08179","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 10 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"12450384","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16026156","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1MEN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1ZLY","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"12755606","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"1NJS","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI4 |
Number of Residues | 14 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"12755606","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"16026156","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"1NJS","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1ZLY","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | Site: {"description":"Raises pKa of active site His","evidences":[{"source":"UniProtKB","id":"P08179","evidenceCode":"ECO:0000250"}]} |
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 | THR135 | |
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 | THR135 | |
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 |