Structure of PDB 3lhl Chain A

Receptor sequence
>3lhlA (length=276) Species: 272563 (Clostridioides difficile 630) [Search protein sequence]
NYEESNLIVFGVGFDGTTSNRPGARFASSSMRKEFYGLETYSPFLDLDLE
DYNICDYGDLEISVGSTEQVLKEIYQETYKIVRDSKVPFMIGGEHLVTLP
AFKAVHEKYNDIYVIHFDAHTDLREEYNNSKNSHATVIKRIWDIVGDNKI
FQFGIRSGTKEEFKFATEEKHTYMEIGGIDTFENIVNMLNGKNIYLTIDL
DVLDASVFPGTGTPEPGGVNYREFQEIFKIIKNSNINIVGCDIVELSPDY
DTTGVSTVIACKILRELCLIISDKIK
3D structure
PDB3lhl Crystal structure of a putative agmatinase from Clostridium difficile
ChainA
Resolution2.3 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H111 D134 H136 D138 H150 D215 D217 E261
Catalytic site (residue number reindexed from 1) H95 D118 H120 D122 H134 D199 D201 E245
Enzyme Commision number 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 A H111 D134 D138 D215 H95 D118 D122 D199
BS02 MN A D134 H136 D215 D217 D118 H120 D199 D201
BS03 MN A D138 H150 D122 H134
Gene Ontology
Molecular Function
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:0033389 putrescine biosynthetic process from arginine, using agmatinase

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Molecular Function
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Biological Process
External links
PDB RCSB:3lhl, PDBe:3lhl, PDBj:3lhl
PDBsum3lhl
PubMed
UniProtQ18A84

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