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1RC0

Human GAR Tfase complex structure with polyglutamated 10-(trifluoroacetyl)-5,10-dideazaacyclic-5,6,7,8-tetrahydrofolic acid

Functional Information from GO Data
ChainGOidnamespacecontents
A0004644molecular_functionphosphoribosylglycinamide formyltransferase activity
A0006189biological_process'de novo' IMP biosynthetic process
A0009058biological_processbiosynthetic process
B0004644molecular_functionphosphoribosylglycinamide formyltransferase activity
B0006189biological_process'de novo' IMP biosynthetic process
B0009058biological_processbiosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues17
DetailsBINDING SITE FOR RESIDUE KT5 A 510
ChainResidue
AARG64
ASER118
AVAL139
AALA140
AGLU141
AVAL143
AASP144
AHOH538
AHOH572
AMET89
AARG90
AILE91
ALEU92
AASN106
AHIS108
APRO109
AGLY117

site_idAC2
Number of Residues23
DetailsBINDING SITE FOR RESIDUE KT5 B 610
ChainResidue
BARG64
BMET89
BARG90
BILE91
BLEU92
BVAL97
BASN106
BHIS108
BPRO109
BGLY117
BSER118
BVAL139
BALA140
BGLU141
BVAL143
BASP144
BHOH613
BHOH620
BHOH641
BHOH657
BHOH666
BHOH684
BHOH702

Functional Information from PROSITE/UniProt
site_idPS00373
Number of Residues24
DetailsGART Phosphoribosylglycinamide formyltransferase active site. GcTVhFVaEdVDaGqiIlqeavpV
ChainResidueDetails
AGLY133-VAL156

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"UniProtKB","id":"P08179","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues10
DetailsBinding 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"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"12755606","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"1NJS","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues14
DetailsBinding 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"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsSite: {"description":"Raises pKa of active site His","evidences":[{"source":"UniProtKB","id":"P08179","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1c2t
ChainResidueDetails
ATHR135
AASN106
AASP144
AHIS108

site_idCSA2
Number of Residues4
DetailsAnnotated By Reference To The Literature 1c2t
ChainResidueDetails
BTHR135
BASN106
BASP144
BHIS108

site_idCSA3
Number of Residues3
DetailsAnnotated By Reference To The Literature 1c2t
ChainResidueDetails
AASN106
AASP144
AHIS108

site_idCSA4
Number of Residues3
DetailsAnnotated By Reference To The Literature 1c2t
ChainResidueDetails
BASN106
BASP144
BHIS108

site_idCSA5
Number of Residues2
DetailsAnnotated By Reference To The Literature 1c2t
ChainResidueDetails
AASP144
AHIS108

site_idCSA6
Number of Residues2
DetailsAnnotated By Reference To The Literature 1c2t
ChainResidueDetails
BASP144
BHIS108

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PDB entries from 2025-07-23

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