Structure of PDB 1gyg Chain A

Receptor sequence

>1gygA (length=370) Species: 1502 (Clostridium perfringens)

WDGKIDGTGTHAMIVTQGVSILENDLSKNEPESVRKNLEILKENMHELQL
GSTYPDYDKNAYDLYQDHFWDPDTDNNFSKDNSWYLAYSIPDTGESQIRK
FSALARYEWQRGNYKQATFYLGEAMHYFGDIDTPYHPANVTAVDSAGHVK
FETFAEERKEQYKINTVGCKTNEDFYADILKNKDFNAWSKEYARGFAKTG
KSIYYSHASMSHSWDDWDYAAKVTLANSQKGTAGYIYRFLHDVSEGNDPS
VGKNVKELVAYISTSGEKDAGTDDYMYFGIKTKDGKTQEWEMDNPGNDFM
TGSKDTYTFKLKDENLKIDDIQNMWIRKRKYTAFPDAYKPENIKVIANGK
VVVDKDINEWISGNSTYNIK

3D structure

• PDB: 1gyg Crystal Structure of the C. Perfringens Alpha-Toxin with the Active Site Closed by a Flexible Loop Region
• Chain: A
• Resolution: 1.9 Å

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	A	D56 H68 H126 D130	D56 H68 H126 D130
BS02	ZN	A	W1 H11 D130	W1 H11 D130

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:0050429 calcium-dependent phospholipase C activity
• 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

External links

• PDB: RCSB:1gyg, PDBe:1gyg, PDBj:1gyg
• PDBsum: 1gyg
• PubMed: 12051905
• UniProt: P0C216|PHLC1_CLOPE Phospholipase C (Gene Name=plc)