Structure of PDB 3hgn Chain A

Receptor sequence
>3hgnA (length=240) Species: 9823 (Sus scrofa) [Search protein sequence]
VVGGTEAQRNSWPSQISLQYRSGSSWAHTCGGTLIRQNWVMTAAHCVDRE
LTFRVVVGEHNLNQNDGTEQYVGVQKIVVHPYWNTDDVAAGYDIALLRLA
QSVTLNSYVQLGVLPRAGTILANNSPCYITGWGLTRTNGQLAQTLQQAYL
PTVDYAICSSSSYWGSTVKNSMVCAGGDGVRSGCQGDSGGPLHCLVNGQY
AVHGVTSFVSRLGCNVTRKPTVFTRVSAYISWINNVIASN
3D structure
PDB3hgn Combined High-Resolution Neutron and X-ray Analysis of Inhibited Elastase Confirms the Active-Site Oxyanion Hole but Rules against a Low-Barrier Hydrogen Bond
ChainA
Resolution1.201 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H57 D102 Q192 G193 D194 S195 G196
Catalytic site (residue number reindexed from 1) H45 D93 Q185 G186 D187 S188 G189
Enzyme Commision number 3.4.21.36: pancreatic elastase.
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 FRW A H57 T175 C191 Q192 G193 D194 S195 S214 F215 V216 R217A H45 T167 C184 Q185 G186 D187 S188 S207 F208 V209 R211
BS02 CA A E70 N72 Q75 D77 E80 E59 N61 Q64 D66 E69
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:3hgn, PDBe:3hgn, PDBj:3hgn
PDBsum3hgn
PubMed19603802
UniProtP00772|CELA1_PIG Chymotrypsin-like elastase family member 1 (Gene Name=CELA1)

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