Structure of PDB 4rw3 Chain A

Receptor sequence

>4rw3A (length=279) Species: 58218 (Loxosceles intermedia)

GNRRPIWIMGHMVNAIGQIDEFVNLGANSIETDVSFDDNANPEYTYHGIP
CDCGRNCKKYENFNDFLKGLRSATTPGNSKYQEKLVLVVFDLKTGSLYDN
QANDAGKKLAKNLLQHYWNNGNNGGRAYIVLSIPDLNHYPLIKGFKDQLT
KDGHPELMDKVGHDFSGNDDIGDVGKAYKKAGITGHIWQSDGITNCLPRG
LSRVNAAVANRDSANGFINKVYYWTVDKRSTTRDALDAGVDGIMTNYPDV
ITDVLNEAAYKKKFRVATYDDNPWVTFKK

3D structure

• PDB: 4rw3 Structural Insights into Substrate Binding of Brown Spider Venom Class II Phospholipases D.
• Chain: A
• Resolution: 1.72 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): H12 E32 D34 H48 G49 D53 D92 K94 W225 D228 N247
• Catalytic site (residue number reindexed from 1): H11 E31 D33 H47 G48 D52 D91 K93 W224 D227 N246
• Enzyme Commision number: 4.6.1.-

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	MG	A	E32 D34 D92	E31 D33 D91
BS02	IPD	A	H12 E32 H48 D92 K94 Y223 W225	H11 E31 H47 D91 K93 Y222 W224
BS03	SHV	A	G176 I184 T185 F218	G175 I183 T184 F217

Gene Ontology

Molecular Function

• GO:0008081 phosphoric diester hydrolase activity
• GO:0016829 lyase activity
• GO:0046872 metal ion binding
• GO:0090729 toxin activity

Biological Process

• GO:0006629 lipid metabolic process
• GO:0016042 lipid catabolic process
• GO:0031640 killing of cells of another organism
• GO:0035821 modulation of process of another organism

Cellular Component

• GO:0005576 extracellular region

External links

• PDB: RCSB:4rw3, PDBe:4rw3, PDBj:4rw3
• PDBsum: 4rw3
• PubMed: 25961401
• UniProt: P0CE82|A1HB2_LOXIN Dermonecrotic toxin LiSicTox-alphaIA1bii (Fragment)