Structure of PDB 1men Chain C

Receptor sequence
>1menC (length=201) Species: 9606 (Homo sapiens) [Search protein sequence]
RILVAVLISGTGSNLQALIDSTREPNSSAQIDIVISNKAAVAGLDKAERA
GIPTRVINHKLYKNRVEFDSAIDLVLEEFSIDIVCLAGFMRILSGPFVQK
WNGKMLNIHPSLLPSFKGSNAHEQALETGVTVTGCTVHFVAEDVDAGQII
LQEAVPVKRGDTVATLSERVKLAEHKIFPAALQLVASGTVQLGENGKICW
V
3D structure
PDB1men Crystal structures of human GAR Tfase of low and high pH and with substrate beta-GAR
ChainC
Resolution2.23 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) N107 H109 T136 D145
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 GAR C G11 S12 N13 M89 I107 P109 K170 E173 G12 S13 N14 M90 I108 P110 K171 E174
Gene Ontology
Molecular Function
GO:0004644 phosphoribosylglycinamide formyltransferase activity
Biological Process
GO:0006189 'de novo' IMP biosynthetic process
GO:0009058 biosynthetic process

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Molecular Function
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Biological Process
External links
PDB RCSB:1men, PDBe:1men, PDBj:1men
PDBsum1men
PubMed12450384
UniProtP22102|PUR2_HUMAN Trifunctional purine biosynthetic protein adenosine-3 (Gene Name=GART)

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