Structure of PDB 2ys6 Chain A

Receptor sequence
>2ys6A (length=421) Species: 1462 (Geobacillus kaustophilus) [Search protein sequence]
NLYFQSHMNVLVIGRGGREHAIAWKAAQSPLVGKLYVAPGNPGIADVAEL
VHIDELDIEALVQFAKQQAIDLTIVGPEAPLASGIVDRFMAEGLRIFGPS
QRAALIEGSKAFAKELMKKYGIPTADHAAFTSYEEAKAYIEQKGAPIVIK
ADGKGVTVAQTVEEALAAAKAALVDGQFGTAGSQVVIEEYLEGEEFSFMA
FVNGEKVYPLAIAQDHKRAYDGDEGPNTGGMGAYSPVPQISDEMMDAALE
AILRPAAKALAAEGRPFLGVLYAGLMATANGPKVIEFNARFGDPEAQVVL
PRLKTDLVEAVLAVMDGKELELEWTDEAVLGVVLAAKGYPGAYERGAEIR
GLDRISPDALLFHAGTKREGGAWYTNGGRVLLLAAKGETLAKAKEKAYEQ
LAAIDCDGLFYRRDIGRRAIE
3D structure
PDB2ys6 Crystal structures of glycinamide ribonucleotide synthetase, PurD, from thermophilic eubacteria
ChainA
Resolution2.21 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 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 GLY A D212 G226 Y269 R287 D290 E292 D215 G229 Y272 R290 D293 E295
BS02 AMP A E192 K214 I282 E195 K217 I285
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0004637 phosphoribosylamine-glycine ligase activity
GO:0005524 ATP binding
GO:0016874 ligase activity
GO:0046872 metal ion binding
Biological Process
GO:0006164 purine nucleotide biosynthetic 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:2ys6, PDBe:2ys6, PDBj:2ys6
PDBsum2ys6
PubMed20716513
UniProtQ5L3C7

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