Structure of PDB 1gym Chain A

Receptor sequence
>1gymA (length=296) Species: 1396 (Bacillus cereus) [Search protein sequence]
ASSVNELENWSKWMQPIPDSIPLARISIPGTHDSGTFKLQNPIKQVWGMT
QEYDFRYQMDHGARIFDIRGRLTDDNTIVLHHGPLYLYVTLHEFINEAKQ
FLKDNPSETIIMSLKKEYEDMKGAEDSFSSTFEKKYFVDPIFLKTEGNIK
LGDARGKIVLLKRYSGSNEPGGYNNFYWPDNETFTTTVNQNANVTVQDKY
KVSYDEKVKSIKDTMDETMNNSEDLNHLYINFTSLSSGGTAWNSPYYYAS
YINPEIANYIKQKNPARVGWVIQDYINEKWSPLLYQEVIRANKSLI
3D structure
PDB1gym Crystal structure of phosphatidylinositol-specific phospholipase C from Bacillus cereus in complex with glucosaminyl(alpha 1-->6)-D-myo-inositol, an essential fragment of GPI anchors.
ChainA
Resolution2.2 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H32 D33 R69 H82 D274
Catalytic site (residue number reindexed from 1) H32 D33 R69 H82 D274
Enzyme Commision number 4.6.1.13: phosphatidylinositol diacylglycerol-lyase.
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 MYG A H32 R69 K115 R163 D198 Y200 H32 R69 K115 R163 D198 Y200 MOAD: ic50=2mM
PDBbind-CN: -logKd/Ki=2.70,IC50=2mM
Gene Ontology
Molecular Function
GO:0004436 phosphatidylinositol diacylglycerol-lyase activity
GO:0008081 phosphoric diester hydrolase activity
GO:0016829 lyase activity
Biological Process
GO:0006629 lipid metabolic process
GO:0016042 lipid catabolic process
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:1gym, PDBe:1gym, PDBj:1gym
PDBsum1gym
PubMed8755729
UniProtP14262|PLC_BACCE 1-phosphatidylinositol phosphodiesterase

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