Structure of PDB 7lox Chain B

Receptor sequence
>7loxB (length=283) Species: 562 (Escherichia coli) [Search protein sequence]
AFGFLRLPMNFQPYDSDADWVITGVPFDGGRHGPAAIRQVSTNLAWEHNR
FPWNFDMRERLNVVDCGDLVYAFGDAREMSEKLQAHAEKLLAAGKRMLSF
GGDHFVTLPLLRAHAKHFGKMALVHFDAHTDTYANGCEFDHGTMFYTAPK
EGLIDPNHSVQIGIRTEFDKDNGFTVLDACQVNDRSVDDVIAQVKQIVGD
MPVYLTFDIDCLDPAFAPGTGTPVIGGLTSDRAIKLVRGLKDLNIVGMDV
VEVAPAYDQSEITALAAATLALEMLYIQAAKKG
3D structure
PDB7lox Crystal Structure of Escherichia coli Agmatinase: Catalytic Mechanism and Residues Relevant for Substrate Specificity.
ChainB
Resolution3.2 Å
3D
structure
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Enzymatic activity
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 B D149 H151 D230 D232 D127 H129 D208 D210
BS02 MN B H126 D149 D153 D230 H104 D127 D131 D208
BS03 GAI B H126 H151 D153 H163 D230 D232 H104 H129 D131 H141 D208 D210
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

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:7lox, PDBe:7lox, PDBj:7lox
PDBsum7lox
PubMed33946272
UniProtP60651|SPEB_ECOLI Agmatinase (Gene Name=speB)

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