1DFN

CRYSTAL STRUCTURE OF DEFENSIN HNP-3, AN AMPHIPHILIC DIMER: MECHANISMS OF MEMBRANE PERMEABILIZATION

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005576	cellular_component	extracellular region
A	0006952	biological_process	defense response
B	0005576	cellular_component	extracellular region
B	0006952	biological_process	defense response

Functional Information from PROSITE/UniProt

site_id	PS00269
Number of Residues	29
Details	DEFENSIN Mammalian defensins signature. CyCripa.CiagerryGtCiyqgrlwafCC

Chain	Residue	Details
A	CYS3-CYS31

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	56
Details	Peptide: {"description":"Neutrophil defensin 2","featureId":"PRO_0000006780"}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	4
Details	Modified residue: {"description":"ADP-ribosylarginine; by ART1","evidences":[{"source":"PubMed","id":"21904558","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI3
Number of Residues	2
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"21904558","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI4
Number of Residues	58
Details	Peptide: {"description":"Neutrophil defensin 3","featureId":"PRO_0000006779"}

Chain

Residue

Details

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