Structure of PDB 3pzl Chain A

Receptor sequence
>3pzlA (length=290) Species: 273116 (Thermoplasma volcanium GSS1) [Search protein sequence]
ASELRSIFSLKKIADAVNGYEEAKYVVFGIPFDNTSSYRRGSKYAPDSIR
GAYVNLESYEYSYGIDLLASGMADLGDMEESEDVEYVIDTVESVVSAVMS
DGKIPIMLGGEHSITVGAVRALPKDVDLVIVDAHSDFRSSYMGNKYNHAC
VTRRALDLLGEGRITSIGIRSVSREEFEDPDFRKVSFISSFDVKKNGIDK
YIEEVDRKSRRVYISVDMDGIDPAYAPAVGTPEPFGLADTDVRRLIERLS
YKAVGFDIVEFSPLYDNGNTSMLAAKLLQVFIASREKYYK
3D structure
PDB3pzl The crystal structure of agmatine ureohydrolase of Thermoplasma volcanium
ChainA
Resolution2.7 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H124 D144 H146 D148 H160 D229 D231 E272
Catalytic site (residue number reindexed from 1) H112 D132 H134 D136 H148 D217 D219 E260
Enzyme Commision number ?
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 H124 D144 D148 D229 H112 D132 D136 D217
BS02 MN A D144 H146 D229 D231 D132 H134 D217 D219
Gene Ontology
Molecular Function
GO:0003824 catalytic 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:0033389 putrescine biosynthetic process from arginine, using agmatinase

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Molecular Function
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Biological Process
External links
PDB RCSB:3pzl, PDBe:3pzl, PDBj:3pzl
PDBsum3pzl
PubMed
UniProtQ97BB8

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