Structure of PDB 1kho Chain B

Receptor sequence
>1khoB (length=370) Species: 1502 (Clostridium perfringens) [Search protein sequence]
WDGKADGTGTHAMIATQGVTILENDLSSNEPEVIRNNLEILKQNMHDLQL
GSTYPDYDKNAYDLYQDHFWDPDTDNNFTKDSKWYLSYSIPDTAESQIRK
FSALARYEWKRGNYKQATFYLGEAMHYFGDADTPYHAANVTAVDSPGHVK
FETFAEDRKDQYKINTTGSKTNDAFYSNILTNEDFNSWSKEFARSFAKTA
KDLYYSHANMSCSWDEWDYAAKVALANSQKGTSGYIYRFLHDVSDGKDSS
ANKNVNELVAYITTGGEKYAGTDDYMYFGIKTKDGQTQEWTMDNPGNDFM
TGSQDTYTFKLKDKNLKIDDIQNMWIRKSKYTEFGDDYKPANIKVIANGN
VVLNKDINEWISGNSTYNIK
3D structure
PDB1kho The first strain of Clostridium perfringens isolated from an avian source has an alpha-toxin with divergent structural and kinetic properties.
ChainB
Resolution2.4 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 H126 D130 H136 H148 E152
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 D130
BS02 ZN B D56 H68 H126 D130 D56 H68 H126 D130
BS03 ZN B H136 H148 E152 H136 H148 E152
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
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:1kho, PDBe:1kho, PDBj:1kho
PDBsum1kho
PubMed12009886
UniProtQ9RF12|PHLC_CLOPF Phospholipase C (Gene Name=plc)

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