Structure of PDB 1wog Chain E

Receptor sequence
>1wogE (length=303) Species: 1299 (Deinococcus radiodurans) [Search protein sequence]
GPAHLPYGGIPTFARAPLVQPDGDWQADVAALGVPFDIALGFRPGARFAP
RALREASLRSVPPFTGLDGKTRLQGVTFADAGDVILPSLEPQLAHDRITE
AARQVRGRCRVPVFLGGDHSVSYPLLRAFADVPDLHVVQLDAHLDFTDTR
NDTKWSNSSPFRRACEALPNLVHITTVGLRGLRFDPEAVAAARARGHTII
PMDDVTADLAGVLAQLPRGQNVYFSVDVDGFDPAVIPGTSSPEPDGLTYA
QGMKILAAAAANNTVVGLDLVELAPNLDPTGRSELLMARLVMETLCEVFD
HVL
3D structure
PDB1wog Crystal structure of agmatinase reveals structural conservation and inhibition mechanism of the ureohydrolase superfamily
ChainE
Resolution1.8 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H121 D143 H145 D147 N159 D229 D231 E274
Catalytic site (residue number reindexed from 1) H119 D141 H143 D145 N157 D227 D229 E272
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 E H121 D143 D147 D229 H119 D141 D145 D227
BS02 MN E D143 H145 D229 D231 D141 H143 D227 D229
BS03 16D E H145 D147 N159 S160 H143 D145 N157 S158
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:1wog, PDBe:1wog, PDBj:1wog
PDBsum1wog
PubMed15355972
UniProtQ9RZ04

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