Structure of PDB 5h8i Chain G

Receptor sequence
>5h8iG (length=295) Species: 3880 (Medicago truncatula) [Search protein sequence]
RKVVVSALQFACTDDVSTNVTTAERLVRAAHKQGANIVLIQELFEGYYFC
QAQREDFIQRAKPYKDHPTIMRLQKLAKELGVVIPVSFFEEANNAHYNSI
AIIDADGTDLGIYRKSHIPDGPGYEEKFYFNPGDTGFKVFQTKYAKIGVA
ICWDQWFPEAARAMALQGAEILFYPTAIGSEPHDQSIDSRDHWKRVMQGH
AGANLVPLVASNRIGNEIIETEHGKSEIKFYGNSFIAGPTGEIVSIADDK
EEAVLIAEFNLDKIKSMRHCWGVFRDRRPDLYKVLLTLDGKNPVL
3D structure
PDB5h8i Structural Investigations of N-carbamoylputrescine Amidohydrolase from Medicago truncatula: Insights into the Ultimate Step of Putrescine Biosynthesis in Plants.
ChainG
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) E42 N98 K115 E126 C152 A177
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 G E48 Y54 P125 Y130 C158 W159 A183 E187 E42 Y48 P119 Y124 C152 W153 A177 E181
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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