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5J9F

Human GAR transformylase in complex with GAR and (4-{[2-(2-Amino-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidin-6-yl)ethyl]amino}benzoyl)-L-glutamic acid (AGF183)

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 Residues15
Detailsbinding site for residue GAR A 1101
ChainResidue
ATHR817
AHOH1201
AHOH1207
AHOH1208
AHOH1209
AHOH1211
AHOH1234
AGLY818
ASER819
AASN820
AGLY894
APRO916
ALYS977
AGLU980
A83A1102

site_idAC2
Number of Residues16
Detailsbinding site for residue 83A A 1102
ChainResidue
APHE895
AMET896
AARG897
AILE898
ALEU899
AVAL904
AASN913
AHIS944
AVAL946
AALA947
AGLU948
AVAL950
AASP951
AGAR1101
AHOH1201
AHOH1205

Functional Information from PROSITE/UniProt
site_idPS00373
Number of Residues24
DetailsGART Phosphoribosylglycinamide formyltransferase active site. GcTVhFVaEdVDaGqiIlqeavpV
ChainResidueDetails
AGLY940-VAL963

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000250|UniProtKB:P08179
ChainResidueDetails
AHIS915

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
AGLY818
ALYS977

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000305|PubMed:12755606, ECO:0007744|PDB:1NJS
ChainResidueDetails
AARG871
AASN913

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
AMET896
AALA947

site_idSWS_FT_FI5
Number of Residues1
DetailsSITE: Raises pKa of active site His => ECO:0000250|UniProtKB:P08179
ChainResidueDetails
AASP951

222926

PDB entries from 2024-07-24

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