Structure of PDB 4pxd Chain B

Receptor sequence

>4pxdB (length=411) Species: 83333 (Escherichia coli K-12)

MITHFRQAIEETLPWLSSFGADPAGGMTRLLYSPEWLETQQQFKKRMAAS
GLETRFDEVGNLYGRLNGTEYPQEVVLSGSHIDTVVNGGNLDGQFGALAA
WLAIDWLKTQYGAPLRTVEVVAMAEAEGSRFPYVFWGSKNIFGLANPDDV
RNICDAKGNSFVDAMKACGFTLPNAPLTPRQDIKAFVELHIEQGCVLESN
GQSIGVVNAIVGQRRYTVTLNGESNHAGTTPMGYRRDTVYAFSRICHQSV
EKAKRMGDPLVLTFGKVEPRPNTVNVVPGKTTFTIDCRHTDAAVLRDFTQ
QLENDMRAICDEMDIGIDIDLWMDEEPVPMNKELVATLTELCEREKLNYR
VMHSGAGHDAQIFAPRVPTCMIFIPSINGISHNPAERTNITDLAEGVKTL
ALMLYQLAWQK

3D structure

• PDB: 4pxd Structural insights into the substrate specificity of (s)-ureidoglycolate amidohydrolase and its comparison with allantoate amidohydrolase.
• Chain: B
• Resolution: 2.2 Å

Enzymatic activity

• Enzyme Commision number: 3.5.3.9: allantoate deiminase.

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	1AL	B	H226 N275	H226 N275
BS02	MN	B	D92 E127 H382	D92 E127 H382
BS03	1AL	B	D92 A126 F135 H190 Q193 Q213 R215 R288 A356 G357	D92 A126 F135 H190 Q193 Q213 R215 R288 A356 G357

Gene Ontology

Molecular Function

• GO:0008270 zinc ion binding
• 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:0042803 protein homodimerization activity
• GO:0046872 metal ion binding
• GO:0047652 allantoate deiminase activity

Biological Process

• GO:0000256 allantoin catabolic process
• GO:0006144 purine nucleobase metabolic process
• GO:0009442 allantoin assimilation pathway

Cellular Component

• GO:0005737 cytoplasm

External links

• PDB: RCSB:4pxd, PDBe:4pxd, PDBj:4pxd
• PDBsum: 4pxd
• PubMed: 25020232
• UniProt: P77425|ALLC_ECOLI Allantoate amidohydrolase (Gene Name=allC)