Structure of PDB 1ela Chain A

Receptor sequence
>1elaA (length=240) Species: 9823 (Sus scrofa) [Search protein sequence]
VVGGTEAQRNSWPSQISLQYRSGSSWAHTCGGTLIRQNWVMTAAHCVDRE
LTFRVVVGEHNLNQNNGTEQYVGVQKIVVHPYWNTDDVAAGYDIALLRLA
QSVTLNSYVQLGVLPRAGTILANNSPCYITGWGLTRTNGQLAQTLQQAYL
PTVDYAICSSSSYWGSTVKNSMVCAGGDGVRSGCQGDSGGPLHCLVNGQY
AVHGVTSFVSRLGCNVTRKPTVFTRVSAYISWINNVIASN
3D structure
PDB1ela Analogous inhibitors of elastase do not always bind analogously.
ChainA
Resolution2.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H60 D108 Q200 G201 D202 S203 G204
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 0Z1 A H60 V103 A104 C199 Q200 S203 S222 F223 V224 H45 V88 A89 C184 Q185 S188 S207 F208 V209 MOAD: Ki=0.44uM
PDBbind-CN: -logKd/Ki=6.36,Ki=0.44uM
BS02 CA A E74 N76 Q79 N81 E84 E59 N61 Q64 N66 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:1ela, PDBe:1ela, PDBj:1ela
PDBsum1ela
PubMed7656008
UniProtP00772|CELA1_PIG Chymotrypsin-like elastase family member 1 (Gene Name=CELA1)

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