Structure of PDB 6vst Chain K

Receptor sequence
>6vstK (length=318) Species: 3880 (Medicago truncatula) [Search protein sequence]
SPALLEKAQNRVIDAALTFIRERAKFKGELMRSLGGVAATSSLLGVPLGH
HSSFHEGSAFAPPRIREAIWCDSTNSTTEEGKNLRDPRVITNVGDVPIEE
IRDCGVDDKRLANVISESVKLVMDEDPLRPLVLGGDHSISFPVVRAVSEK
LGGAVDILHFDAHPDLYHDFEGNYYSHASPFARIMEGGYARRLVQVGIRS
ITNDVREQVKKYGVETHEMRTLSRDRPILENLKLGEGVKGVYVSIDVDSL
DPSIAPGVSHHEPGGLLFRDILNILQNLQGDIVGGDVVEYNPQRDTYDGI
TALVAAKLVRELAAKMSK
3D structure
PDB6vst The Neighboring Subunit Is Engaged to Stabilize the Substrate in the Active Site of Plant Arginases.
ChainK
Resolution2.12 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 3.5.3.1: arginase.
3.5.3.11: agmatinase.
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 MN K D181 H183 D266 D268 D161 H163 D246 D248
BS02 MN K H157 D181 D185 D266 H137 D161 D165 D246
Gene Ontology
Molecular Function
GO:0004053 arginase activity
GO:0008783 agmatinase activity
GO:0016787 hydrolase activity
GO:0016813 hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines
GO:0046872 metal ion binding
Biological Process
GO:0000050 urea cycle
GO:0006525 arginine metabolic process
GO:0009446 putrescine biosynthetic process
GO:0019547 arginine catabolic process to ornithine
GO:0033388 putrescine biosynthetic process from arginine
GO:0033389 putrescine biosynthetic process from arginine, using agmatinase
GO:0034214 protein hexamerization
Cellular Component
GO:0005739 mitochondrion

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:6vst, PDBe:6vst, PDBj:6vst
PDBsum6vst
PubMed32754173
UniProtG7JFU5|ARGI_MEDTR Arginase, mitochondrial (Gene Name=ARGAH)

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