Structure of PDB 5h8i Chain E

Receptor sequence
>5h8iE (length=297) Species: 3880 (Medicago truncatula) [Search protein sequence]
KGRKVVVSALQFACTDDVSTNVTTAERLVRAAHKQGANIVLIQELFEGYY
FCQAQREDFIQRAKPYKDHPTIMRLQKLAKELGVVIPVSFFEEANNAHYN
SIAIIDADGTDLGIYRKSHIPDGPGYEEKFYFNPGDTGFKVFQTKYAKIG
VAICWDQWFPEAARAMALQGAEILFYPTAIGSEPHDQSIDSRDHWKRVMQ
GHAGANLVPLVASNRIGNEIIETEHGKSEIKFYGNSFIAGPTGEIVSIAD
DKEEAVLIAEFNLDKIKSMRHCWGVFRDRRPDLYKVLLTLDGKNPVL
3D structure
PDB5h8i Structural Investigations of N-carbamoylputrescine Amidohydrolase from Medicago truncatula: Insights into the Ultimate Step of Putrescine Biosynthesis in Plants.
ChainE
Resolution1.97 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) E48 N104 K121 E132 C158 A183
Catalytic site (residue number reindexed from 1) E44 N100 K117 E128 C154 A179
Enzyme Commision number 3.5.1.53: N-carbamoylputrescine amidase.
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 N2H E E48 Y54 P125 Y130 C158 W159 A183 E187 E44 Y50 P121 Y126 C154 W155 A179 E183
Gene Ontology
Molecular Function
GO:0016787 hydrolase activity
GO:0016810 hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
GO:0050126 N-carbamoylputrescine amidase activity
Biological Process
GO:0006596 polyamine biosynthetic process
GO:0033388 putrescine biosynthetic process from arginine

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Molecular Function
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Biological Process
External links
PDB RCSB:5h8i, PDBe:5h8i, PDBj:5h8i
PDBsum5h8i
PubMed27066023
UniProtG7ITU5

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