Structure of PDB 2wy6 Chain B

Receptor sequence
>2wy6B (length=365) Species: 1502 (Clostridium perfringens) [Search protein sequence]
WDGKIDGTGTHAMIVTQGVSILENDLSKNEPESVRKNLEILKENMHELQL
GSTYPDYDKNAYDLYQDHFWDPDIDDNSWYLAYSIPDTGESQIRKFSALA
RYEWQRGNYKQATFYLGEAMHYFGDIDTPYHPANVTAVDSAGHVKFETFA
EERKEQYKINTAGCKTNEAFYTDILKNKDFNAWSKEYARGFAKTGKSIYY
SHASMSHSWDDWDYAAKVTLANSQKGTAGYIYRFLHDVSEGNDPSVGKNV
KELVAYISTSGEKDAGTDDYMYFGIKTKDGKTQEWEMDNPGNDFMTGSKD
TYTFKLKDENLKIDDIQNMWIRKRKYTAFPDAYKPENIKIIANGKVVVDK
DINEWISGNSTYNIK
3D structure
PDB2wy6 Comparison of a Nontoxic Variant of Clostridium Perfringens [Alpha]-Toxin with the Toxic Wild-Type Strain
ChainB
Resolution3.2 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H11 D56 H68 H126 D130 H136 H148 E152
Catalytic site (residue number reindexed from 1) H11 D56 H68 H121 D125 H131 H143 E147
Enzyme Commision number 3.1.4.3: phospholipase C.
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 ZN B W1 H11 D130 W1 H11 D125
BS02 CA B D293 G296 D298 D288 G291 D293
BS03 CA B D269 G271 D336 A337 D264 G266 D331 A332
Gene Ontology
Molecular Function
GO:0004629 phospholipase C activity
GO:0008270 zinc ion binding
GO:0016787 hydrolase activity
GO:0016788 hydrolase activity, acting on ester bonds
GO:0034480 phosphatidylcholine phospholipase C activity
GO:0046872 metal ion binding
GO:0090729 toxin activity
Biological Process
GO:0031640 killing of cells of another organism
GO:0035821 modulation of process of another organism
GO:0044179 hemolysis in another organism
Cellular Component
GO:0005576 extracellular region

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:2wy6, PDBe:2wy6, PDBj:2wy6
PDBsum2wy6
PubMed20944240
UniProtQ0TV31|PHLC_CLOP1 Phospholipase C (Gene Name=plc)

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