Structure of PDB 1l1g Chain A Binding Site BS02

Receptor Information
>1l1g Chain A (length=240) Species: 9823 (Sus scrofa) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
VVGGTEAQRNSWPSQISLQYRSGSSWAHTCGGTLIRQNWVMTAAHCVDRE
LTFRVVVGEHNLNQNDGTEQYVGVQKIVVHPYWNTDDVAAGYDIALLRLA
QSVTLNSYVQLGVLPRAGTILANNSPCYITGWGLTRTNGQLAQTLQQAYL
PTVDYAICSSSSYWGSTVKNSMVCAGGDGVRSGCQGDSGGPLHCLVNGQY
AVHGVTSFVSRLGCNVTRKPTVFTRVSAYISWINNVIASN
Ligand information
Ligand IDXE
InChIInChI=1S/Xe
InChIKeyFHNFHKCVQCLJFQ-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04
CACTVS 3.341
OpenEye OEToolkits 1.5.0		[Xe]
FormulaXe
NameXENON
ChEMBLCHEMBL1236802
DrugBankDB13453
ZINC
PDB chain1l1g Chain A Residue 261 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1l1g Xenon derivatization of halide-soaked protein crystals.
Resolution1.5 Å
Binding residue
(original residue number in PDB)		C184 F208 V209
Binding residue
(residue number reindexed from 1)		C184 F208 V209
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) H45 D93 Q185 G186 D187 S188 G189
Catalytic site (residue number reindexed from 1) H45 D93 Q185 G186 D187 S188 G189
Enzyme Commision number 3.4.21.36: pancreatic elastase.
Gene Ontology
Molecular Function
GO:0004252 serine-type endopeptidase activity
GO:0005515 protein binding
GO:0008236 serine-type peptidase activity
GO:0046872 metal ion binding
Biological Process
GO:0006508 proteolysis
Cellular Component
GO:0005576 extracellular region
GO:0005615 extracellular space

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1l1g, PDBe:1l1g, PDBj:1l1g
PDBsum1l1g
PubMed12198297
UniProtP00772|CELA1_PIG Chymotrypsin-like elastase family member 1 (Gene Name=CELA1)

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