Structure of PDB 1njs Chain B

Receptor sequence
>1njsB (length=200) Species: 9606 (Homo sapiens) [Search protein sequence]
ARVAVLISGTGSNLQALIDSTREPNSSAQIDIVISNKAAVAGLDKAERAG
IPTRVINHKLYKNRVEFDSAIDLVLEEFSIDIVCLAGFMRILSGPFVQKW
NGKMLNIHPSLLPSFKGSNAHEQALETGVTVTGCTVHFVAEDVDAGQIIL
QEAVPVKRGDTVATLSERVKLAEHKIFPAALQLVASGTVQLGENGKICWV
3D structure
PDB1njs Rational Design, Synthesis, Evaluation, and Crystal Structure of a Potent Inhibitor of Human GAR Tfase: 10-(Trifluoroacetyl)-5,10-dideazaacyclic-5,6,7,8-tetrahydrofolic Acid
ChainB
Resolution1.98 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) N106 H108 T135 D144
Catalytic site (residue number reindexed from 1) N106 H108 T135 D144
Enzyme Commision number 2.1.2.2: phosphoribosylglycinamide formyltransferase 1.
6.3.3.1: phosphoribosylformylglycinamidine cyclo-ligase.
6.3.4.13: phosphoribosylamine--glycine ligase.
Interaction with ligand
Site
#
Ligand Ligand
chain
Binding residues on receptor
(original residue number in PDB)
Binding residues on receptor
(residue number reindexed from 1)
Binding affinity
BS01 KEU B R64 L85 M89 R90 I91 L92 N106 H108 G117 V139 A140 V143 D144 R64 L85 M89 R90 I91 L92 N106 H108 G117 V139 A140 V143 D144 MOAD: Ki=15nM
Gene Ontology
Molecular Function
GO:0004644 phosphoribosylglycinamide formyltransferase activity
Biological Process
GO:0006189 'de novo' IMP biosynthetic process
GO:0009058 biosynthetic process

View graph for
Molecular Function

View graph for
Biological Process
External links
PDB RCSB:1njs, PDBe:1njs, PDBj:1njs
PDBsum1njs
PubMed12755606
UniProtP22102|PUR2_HUMAN Trifunctional purine biosynthetic protein adenosine-3 (Gene Name=GART)

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