Structure of PDB 4pxe Chain B

Receptor sequence

>4pxeB (length=423) Species: 3702 (Arabidopsis thaliana)

NLASSLSVDAPGLQNQIDELSSFSDAPSPSVTRVLYTDKDVSARRYVKNL
MALAGLTVREDAVGNIFGKWDGLEPNLPAVATGSHIDAIPYSGKYDGVVG
VLGAIEAINVLKRSGFKPKRSLEIILFTSEEPTRFGISCLGSRLLAGSKE
LAEALKTTVVDGQNVSFIEAARSAGYAEDKDDDLSSVFLKKGSYFAFLEL
HIEQGPILEDEGLDIGVVTAIAAPASLKVEFEGNGGHAGAVLMPYRNDAG
LAAAELALAVEKHVLESESIDTVGTVGILELHPGAINSIPSKSHLEIDTR
DIDEARRNTVIKKIQESANTIAKKRKVKLSEFKIVNQDPPALSDKLVIKK
MAEAATELNLSHKMMISRAYHDSLFMARISPMGMIFIPCYKGYSHKPEEY
SSPEDMANGVKVLSLTLAKLSLD

3D structure

• PDB: 4pxe Structural insights into the substrate specificity of (s)-ureidoglycolate amidohydrolase and its comparison with allantoate amidohydrolase.
• Chain: B
• Resolution: 1.449 Å

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	GLV	B	H290 N340	H237 N287
BS02	MN	B	H138 D149 H254	H85 D96 H201
BS03	MN	B	D149 E184 H448	D96 E131 H395
BS04	GLV	B	E183 R353 A422 Y423	E130 R300 A369 Y370

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

External links

• PDB: RCSB:4pxe, PDBe:4pxe, PDBj:4pxe
• PDBsum: 4pxe
• PubMed: 25020232
• UniProt: Q8VXY9|UAH_ARATH Ureidoglycolate hydrolase (Gene Name=UAH)