Structure of PDB 2qk4 Chain B

Receptor sequence
>2qk4B (length=424) Species: 9606 (Homo sapiens) [Search protein sequence]
SMAARVLIIGSGGREHTLAWKLAQSHHVKQVLVAPGNAGTACSEKISNTA
ISISDHTALAQFCKEKKIEFVVVGPEAPLAAGIVGNLRSAGVQCFGPTAE
AAQLESSKRFAKEFMDRHGIPTAQWKAFTKPEEACSFILSADFPALVVKA
SGLAGVIVAKSKEEACKAVQEIMQEKAGETIVIEELLDGEEVSCLCFTDG
KTVAPMPPAQDHKRLLEGDGGPNTGGMGAYCPAPQVSNDLLLKIKDTVLQ
RTVDGMQQEGTPYTGILYAGIMLTKNGPKVLEFNCRFGDPECQVILPLLK
SDLYEVIQSTLDGLLCTSLPVWLENHTALTVVMASKGYPGDYTKGVEITG
FPEAQALGLEVFHAGTALKNGKVVTHGGRVLAVTAIRENLISALEEAKKG
LAAIKFEGAIYRKDIGFRAIAFLQ
3D structure
PDB2qk4 Structural studies of tri-functional human GART.
ChainB
Resolution2.45 Å
3D
structure
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Enzymatic activity
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 ATP B K148 V160 K162 E190 E191 L193 E197 R220 M278 L287 K149 V158 K160 E184 E185 L187 E191 R214 M272 L281
Gene Ontology
Molecular Function
GO:0004637 phosphoribosylamine-glycine ligase activity
GO:0004641 phosphoribosylformylglycinamidine cyclo-ligase activity
GO:0005524 ATP binding
GO:0046872 metal ion binding
Biological Process
GO:0006189 'de novo' IMP biosynthetic process
GO:0009113 purine nucleobase biosynthetic process

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Molecular Function
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Biological Process
External links
PDB RCSB:2qk4, PDBe:2qk4, PDBj:2qk4
PDBsum2qk4
PubMed20631005
UniProtP22102|PUR2_HUMAN Trifunctional purine biosynthetic protein adenosine-3 (Gene Name=GART)

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