Structure of PDB 6th7 Chain A

Receptor sequence
>6th7A (length=240) Species: 9823 (Sus scrofa) [Search protein sequence]
VVGGTEAQRNSWPSQISLQYRSGSSWAHTCGGTLIRQNWVMTAAHCVDRE
LTFRVVVGEHNLNQNDGTEQYVGVQKIVVHPYWNTDDVAAGYDIALLRLA
QSVTLNSYVQLGVLPRAGTILANNSPCYITGWGLTRTNGQLAQTLQQAYL
PTVDYAICSSSSYWGSTVKNSMVCAGGDGVRSGCQGDSGGPLHCLVNGQY
AVHGVTSFVSRLGCNVTRKPTVFTRVSAYISWINNVIASN
3D structure
PDB6th7 Tutuilamides A-C: Vinyl-Chloride-Containing Cyclodepsipeptides from Marine Cyanobacteria with Potent Elastase Inhibitory Properties.
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) H71 D119 Q211 G212 D213 S214 G215
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 peptide A C56 H71 V114 Q211 G212 S214 S233 F234 V235 S236 R237 C30 H45 V88 Q185 G186 S188 S207 F208 V209 S210 R211
BS02 peptide A W190 S236 R237 W164 S210 R211
BS03 CA A E85 N87 Q90 D92 E95 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:6th7, PDBe:6th7, PDBj:6th7
PDBsum6th7
PubMed31935054
UniProtP00772|CELA1_PIG Chymotrypsin-like elastase family member 1 (Gene Name=CELA1)

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