Structure of PDB 4pxb Chain A

Receptor sequence
>4pxbA (length=423) Species: 3702 (Arabidopsis thaliana) [Search protein sequence]
NLASSLSVDAPGLQNQIDELSSFSDAPSPSVTRVLYTDKDVSARRYVKNL
MALAGLTVREDAVGNIFGKWDGLEPNLPAVATGSHIDAIPYSGKYDGVVG
VLGAIEAINVLKRSGFKPKRSLEIILFTSAEPTRFGISCLGSRLLAGSKE
LAEALKTTVVDGQNVSFIEAARSAGYAEDKDDDLSSVFLKKGSYFAFLEL
HIEQGPILEDEGLDIGVVTAIAAPASLKVEFEGNGGHAGAVLMPYRNDAG
LAAAELALAVEKHVLESESIDTVGTVGILELHPGAINSIPSKSHLEIDTR
DIDEARRNTVIKKIQESANTIAKKRKVKLSEFKIVNQDPPALSDKLVIKK
MAEAATELNLSHKMMISRAYHDSLFMARISPMGMIFIPCYKGYSHKPEEY
SSPEDMANGVKVLSLTLAKLSLD
3D structure
PDB4pxb Structural insights into the substrate specificity of (s)-ureidoglycolate amidohydrolase and its comparison with allantoate amidohydrolase.
ChainA
Resolution1.903 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 3.5.1.116: ureidoglycolate amidohydrolase.
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 MN A H138 D149 G150 H254 H85 D96 G97 H201
BS02 MN A D149 E184 H448 D96 E131 H395
BS03 UGC A E184 H254 Q257 R353 A422 Y423 H424 H448 E131 H201 Q204 R300 A369 Y370 H371 H395
BS04 UGC A H290 N340 H237 N287
Gene Ontology
Molecular Function
GO:0004848 ureidoglycolate hydrolase activity
GO:0016787 hydrolase activity
GO:0016813 hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines
GO:0030145 manganese ion binding
GO:0046872 metal ion binding
GO:0047652 allantoate deiminase activity
Biological Process
GO:0000256 allantoin catabolic process
GO:0006144 purine nucleobase metabolic process
GO:0006145 purine nucleobase catabolic process
GO:0010136 ureide catabolic process
Cellular Component
GO:0005783 endoplasmic reticulum
GO:0009536 plastid

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Cellular Component
External links
PDB RCSB:4pxb, PDBe:4pxb, PDBj:4pxb
PDBsum4pxb
PubMed25020232
UniProtQ8VXY9|UAH_ARATH Ureidoglycolate hydrolase (Gene Name=UAH)

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