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7JG0

Human GAR transformylase in complex with GAR substrate and AGF102 inhibitor

Functional Information from GO Data
ChainGOidnamespacecontents
A0004644molecular_functionphosphoribosylglycinamide formyltransferase activity
A0006189biological_process'de novo' IMP biosynthetic process
A0009058biological_processbiosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues19
Detailsbinding site for residue GAR A 1101
ChainResidue
ATHR816
ALYS976
AGLU979
AV971102
AHOH1206
AHOH1225
AHOH1229
AHOH1237
AHOH1245
AHOH1252
AHOH1255
AGLY817
ASER818
AASN819
AGLY893
AMET895
AHIS914
APRO915
AGLY923

site_idAC2
Number of Residues16
Detailsbinding site for residue V97 A 1102
ChainResidue
AHIS864
AARG870
APHE894
AMET895
AARG896
AILE897
ALEU898
AVAL903
AASN912
AVAL945
AALA946
AGLU947
AVAL949
AASP950
AGAR1101
AHOH1207

Functional Information from PROSITE/UniProt
site_idPS00373
Number of Residues24
DetailsGART Phosphoribosylglycinamide formyltransferase active site. GcTVhFVaEdVDaGqiIlqeavpV
ChainResidueDetails
AGLY939-VAL962

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000250|UniProtKB:P08179
ChainResidueDetails
AHIS914

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:12450384, ECO:0000269|PubMed:16026156, ECO:0007744|PDB:1MEN, ECO:0007744|PDB:1ZLY
ChainResidueDetails
AGLY817
ALYS976

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000305|PubMed:12755606, ECO:0007744|PDB:1NJS
ChainResidueDetails
AARG870
AASN912

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: BINDING => ECO:0000305|PubMed:12755606, ECO:0000305|PubMed:16026156, ECO:0007744|PDB:1NJS, ECO:0007744|PDB:1ZLY
ChainResidueDetails
AMET895
AALA946

site_idSWS_FT_FI5
Number of Residues1
DetailsSITE: Raises pKa of active site His => ECO:0000250|UniProtKB:P08179
ChainResidueDetails
AASP950

223166

PDB entries from 2024-07-31

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