Structure of PDB 3pzl Chain A Binding Site BS02

Receptor Information

>3pzl Chain A (length=290) Species: 273116 (Thermoplasma volcanium GSS1)

ASELRSIFSLKKIADAVNGYEEAKYVVFGIPFDNTSSYRRGSKYAPDSIR
GAYVNLESYEYSYGIDLLASGMADLGDMEESEDVEYVIDTVESVVSAVMS
DGKIPIMLGGEHSITVGAVRALPKDVDLVIVDAHSDFRSSYMGNKYNHAC
VTRRALDLLGEGRITSIGIRSVSREEFEDPDFRKVSFISSFDVKKNGIDK
YIEEVDRKSRRVYISVDMDGIDPAYAPAVGTPEPFGLADTDVRRLIERLS
YKAVGFDIVEFSPLYDNGNTSMLAAKLLQVFIASREKYYK

Ligand information

• Ligand ID: MN
• InChI: InChI=1S/Mn/q+2
• InChIKey: WAEMQWOKJMHJLA-UHFFFAOYSA-N
• SMILES:
  ACDLabs 10.04
  OpenEye OEToolkits 1.5.0: [Mn+2]
  CACTVS 3.341: [Mn++]
• Formula: Mn
• Name: MANGANESE (II) ION
• DrugBank: DB06757
• PDB chain: 3pzl Chain A Residue 315

Receptor-Ligand Complex Structure

Structure summary

• PDB: 3pzl The crystal structure of agmatine ureohydrolase of Thermoplasma volcanium
• Resolution: 2.7 Å
• Binding residue (original residue number in PDB): D144 H146 D229 D231
• Binding residue (residue number reindexed from 1): D132 H134 D217 D219
• Annotation score: 1

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

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

External links

• PDB: RCSB:3pzl, PDBe:3pzl, PDBj:3pzl
• PDBsum: 3pzl
• UniProt: Q97BB8