Structure of PDB 7lox Chain B Binding Site BS02

Receptor Information

>7lox Chain B (length=283) Species: 562 (Escherichia coli)

AFGFLRLPMNFQPYDSDADWVITGVPFDGGRHGPAAIRQVSTNLAWEHNR
FPWNFDMRERLNVVDCGDLVYAFGDAREMSEKLQAHAEKLLAAGKRMLSF
GGDHFVTLPLLRAHAKHFGKMALVHFDAHTDTYANGCEFDHGTMFYTAPK
EGLIDPNHSVQIGIRTEFDKDNGFTVLDACQVNDRSVDDVIAQVKQIVGD
MPVYLTFDIDCLDPAFAPGTGTPVIGGLTSDRAIKLVRGLKDLNIVGMDV
VEVAPAYDQSEITALAAATLALEMLYIQAAKKG

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: 7lox Chain B Residue 402

Receptor-Ligand Complex Structure

Structure summary

• PDB: 7lox Crystal Structure of Escherichia coli Agmatinase: Catalytic Mechanism and Residues Relevant for Substrate Specificity.
• Resolution: 3.2 Å
• Binding residue (original residue number in PDB): H126 D149 D153 D230
• Binding residue (residue number reindexed from 1): H104 D127 D131 D208
• Annotation score: 1

Enzymatic activity

• Enzyme Commision number: 3.5.3.11: agmatinase.

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:0030145 manganese ion binding
• GO:0042802 identical protein binding
• GO:0046872 metal ion binding

Biological Process

• GO:0008295 spermidine biosynthetic process
• GO:0009446 putrescine biosynthetic process
• GO:0033388 putrescine biosynthetic process from arginine
• GO:0033389 putrescine biosynthetic process from arginine, using agmatinase

Cellular Component

• GO:0005829 cytosol

External links

• PDB: RCSB:7lox, PDBe:7lox, PDBj:7lox
• PDBsum: 7lox
• PubMed: 33946272
• UniProt: P60651|SPEB_ECOLI Agmatinase (Gene Name=speB)