Structure of PDB 2f9r Chain D

Receptor sequence
>2f9rD (length=285) Species: 58217 (Loxosceles laeta) [Search protein sequence]
ADNRRPIWNLAHMVNAVAQIPDFLDLGANALEADVTFKGSVPTYTYHGTP
CDFGRDCIRWEYFNVFLKTLREYTTPGNAKYRDGFILFVLDLKTGSLSND
QVRPAGENVAKELLQNYWNNGNNGGRAYVVLSLPDIGHYEFVRGFKEVLK
KEGHEDLLEKVGYDFSGPYLPSLPTLDATHEAYKKAGVDGHIWLSDGLTN
FSPLGDMARLKEAIKSRDSANGFINKIYYWSVDKVSTTKAALDVGVDGIM
TNYPNVLIGVLKESGYNDKYRLATYDDNPWETFKN
3D structure
PDB2f9r Structural basis for metal ion coordination and the catalytic mechanism of sphingomyelinases D.
ChainD
Resolution1.85 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) H12 E32 D34 H47 G48 D52 D91 K93 W230 D233 N252
Catalytic site (residue number reindexed from 1) H12 E32 D34 H47 G48 D52 D91 K93 W230 D233 N252
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 D E32 D34 D91 E32 D34 D91
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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:2f9r, PDBe:2f9r, PDBj:2f9r
PDBsum2f9r
PubMed15654080
UniProtQ8I914|A311_LOXLA Dermonecrotic toxin LlSicTox-alphaIII1i

[Back to BioLiP]