Structure of PDB 2b9l Chain A Binding Site BS01

Receptor Information
>2b9l Chain A (length=372) Species: 33394 (Holotrichia diomphalia) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
GHMAVVNIFGNASEYIPPGYEAPLGALTALPRCGTGADQGKKVCIVYHRC
DGVTNTVTPEEVINTTGEGIFDIRENANECESYLDVCCGLPPVVPVLKPS
FCGIRNERGLDFKITGQTNEAEYGEFPWMVAVLKANEEQLVCGGSLIAPS
VVLTGAHCVNSYQSNLDAIKIRAGEWDTLTEKERLPYQERKIRQVIIHSN
FNPKTVVNDVALLLLDRPLVQADNIGTICLPQQSQIFDSTECFASGWGKK
EFGSRHRYSNILKKIQLPTVDRDKCQADLRNTRLGLKFVLDQTFVCAGGE
QGKDTCTGDGGSPLFCPDPRNPSRYMQMGIVAWGIGCGDENVPGVYANVA
HFRNWIDQEMQAKGLSTTPYVE
Ligand information
Ligand IDCA
InChIInChI=1S/Ca/q+2
InChIKeyBHPQYMZQTOCNFJ-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.341[Ca++]
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Ca+2]
FormulaCa
NameCALCIUM ION
ChEMBL
DrugBankDB14577
ZINC
PDB chain2b9l Chain A Residue 427 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB2b9l Crystal structure of a clip-domain serine protease and functional roles of the clip domains.
Resolution2.0 Å
Binding residue
(original residue number in PDB)		E218 D220 T223 E226
Binding residue
(residue number reindexed from 1)		E175 D177 T180 E183
Annotation score4
Enzymatic activity
Catalytic site (original residue number in PDB) H200 D252 T350 G351 D352 G353 G354
Catalytic site (residue number reindexed from 1) H157 D209 T307 G308 D309 G310 G311
Enzyme Commision number ?
Gene Ontology
Molecular Function
GO:0004252 serine-type endopeptidase activity
GO:0046872 metal ion binding
Biological Process
GO:0006508 proteolysis
GO:0042742 defense response to bacterium
GO:0045087 innate immune response
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:2b9l, PDBe:2b9l, PDBj:2b9l
PDBsum2b9l
PubMed16362048
UniProtQ9GRW0|PPAF2_HOLDI Phenoloxidase-activating factor 2 (Gene Name=PPAF2)

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