Structure of PDB 1rby Chain A

Receptor sequence
>1rbyA (length=200) Species: 9606 (Homo sapiens) [Search protein sequence]
ARVAVLISGTGSNLQALIDSTREPNSSAQIDIVISNKAAVAGLDKAERAG
IPTRVINHKLYKNRVEFDSAIDLVLEEFSIDIVCLAGFMRILSGPFVQKW
NGKMLNIHPSLLPSFKGSNAHEQALETGVTVTGCTVHFVAEDVDAGQIIL
QEAVPVKRGDTVATLSERVKLAEHKIFPAALQLVASGTVQLGENGKICWV
3D structure
PDB1rby Human GAR Tfase complex structure
ChainA
Resolution2.101 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 A R64 M89 R90 I91 L92 N106 H108 G117 S118 V139 A140 E141 V143 D144 R64 M89 R90 I91 L92 N106 H108 G117 S118 V139 A140 E141 V143 D144
BS02 GAR A T10 G11 S12 N13 L85 G87 F88 M89 N106 I107 P109 K170 E173 T10 G11 S12 N13 L85 G87 F88 M89 N106 I107 P109 K170 E173
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:1rby, PDBe:1rby, PDBj:1rby
PDBsum1rby
PubMed
UniProtP22102|PUR2_HUMAN Trifunctional purine biosynthetic protein adenosine-3 (Gene Name=GART)

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