Structure of PDB 5h8l Chain M

Receptor sequence
>5h8lM (length=297) Species: 3880 (Medicago truncatula) [Search protein sequence]
KGRKVVVSALQFACTDDVSTNVTTAERLVRAAHKQGANIVLIQELFEGYY
FCQAQREDFIQRAKPYKDHPTIMRLQKLAKELGVVIPVSFFEEANNAHYN
SIAIIDADGTDLGIYRKSHIPDGPGYEEKFYFNPGDTGFKVFQTKYAKIG
VAISWDQWFPEAARAMALQGAEILFYPTAIGSEPHDQSIDSRDHWKRVMQ
GHAGANLVPLVASNRIGNEIIETEHGKSEIKFYGNSFIAGPTGEIVSIAD
DKEEAVLIAEFNLDKIKSMRHCWGVFRDRRPDLYKVLLTLDGKNPVL
3D structure
PDB5h8l Structural Investigations of N-carbamoylputrescine Amidohydrolase from Medicago truncatula: Insights into the Ultimate Step of Putrescine Biosynthesis in Plants.
ChainM
Resolution2.29 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) E48 N104 K121 E132 S158 A183
Catalytic site (residue number reindexed from 1) E44 N100 K117 E128 S154 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 PUT M Y130 W159 I184 E187 Y126 W155 I180 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

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:5h8l, PDBe:5h8l, PDBj:5h8l
PDBsum5h8l
PubMed27066023
UniProtG7ITU5

[Back to BioLiP]