Structure of PDB 4zyt Chain A

Receptor sequence
>4zytA (length=200) Species: 9606 (Homo sapiens) [Search protein sequence]
ARVAVLISGTGSNLQALIDSTREPNSSAQIDIVISNKAAVAGLDKAERAG
IPTRVINHKLYKNRVEFDSAIDLVLEEFSIDIVCLAGFMRILSGPFVQKW
NGKMLNIHPSLLPSFKGSNAHEQALETGVTVTGCTVHFVAEDVDAGQIIL
QEAVPVKRGDTVATLSERVKLAEHKIFPAALQLVASGTVQLGENGKICWV
3D structure
PDB4zyt Structural and Enzymatic Analysis of Tumor-Targeted Antifolates That Inhibit Glycinamide Ribonucleotide Formyltransferase.
ChainA
Resolution1.702 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
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 G818 S819 N820 M896 P916 K977 E980 G11 S12 N13 M89 P109 K170 E173
BS02 3Y9 A K844 H865 F895 M896 R897 I898 L899 V946 A947 V950 K37 H58 F88 M89 R90 I91 L92 V139 A140 V143 MOAD: Ki=17nM
PDBbind-CN: -logKd/Ki=7.77,Ki=17nM
BindingDB: IC50=6.8nM
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:4zyt, PDBe:4zyt, PDBj:4zyt
PDBsum4zyt
PubMed27439469
UniProtP22102|PUR2_HUMAN Trifunctional purine biosynthetic protein adenosine-3 (Gene Name=GART)

[Back to BioLiP]