Structure of PDB 4zyw Chain A

Receptor sequence
>4zywA (length=200) Species: 9606 (Homo sapiens) [Search protein sequence]
ARVAVLISGTGSNLQALIDSTREPNSSAQIDIVISNKAAVAGLDKAERAG
IPTRVINHKLYKNRVEFDSAIDLVLEEFSIDIVCLAGFMRILSGPFVQKW
NGKMLNIHPSLLPSFKGSNAHEQALETGVTVTGCTVHFVAEDVDAGQIIL
QEAVPVKRGDTVATLSERVKLAEHKIFPAALQLVASGTVQLGENGKICWV
3D structure
PDB4zyw Structural and Enzymatic Analysis of Tumor-Targeted Antifolates That Inhibit Glycinamide Ribonucleotide Formyltransferase.
ChainA
Resolution2.05 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) N913 H915 T942 D951
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 GAR A T817 G818 S819 N820 M896 P916 K977 E980 T10 G11 S12 N13 M89 P109 K170 E173
BS02 G94 A F895 M896 R897 I898 L899 S925 V946 A947 V950 F88 M89 R90 I91 L92 S118 V139 A140 V143 MOAD: Ki=68nM
PDBbind-CN: -logKd/Ki=7.17,Ki=68nM
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:4zyw, PDBe:4zyw, PDBj:4zyw
PDBsum4zyw
PubMed27439469
UniProtP22102|PUR2_HUMAN Trifunctional purine biosynthetic protein adenosine-3 (Gene Name=GART)

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