Structure of PDB 1h9l Chain B

Receptor sequence
>1h9lB (length=240) Species: 9823 (Sus scrofa) [Search protein sequence]
VVGGTEAQRNSWPSQISLQYRSGSSWAHTCGGTLIRQNWVMTAAHCVDRE
LTFRVVVGEHNLNQNNGTEQYVGVQKIVVHPYWNTDDVAAGYDIALLRLA
QSVTLNSYVQLGVLPRAGTILANNSPCYITGWGLTRTNGQLAQTLQQAYL
PTVDYAICSSSSYWGSTVKNSMVCAGGDGVRSGCQGDSGGPLHCLVNGQY
AVHGVTSFVSRLGCNVTRKPTVFTRVSAYISWINNVIASN
3D structure
PDB1h9l Kinetic and Crystallographic Analysis of Complexes Formed between Elastase and Peptides from Beta-Casein
ChainB
Resolution1.67 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
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 peptide B C191 Q192 D194 S195 S214 F215 V216 S217 R217A C184 Q185 D187 S188 S207 F208 V209 S210 R211
BS02 CA B E70 N72 Q75 N77 E80 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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:1h9l, PDBe:1h9l, PDBj:1h9l
PDBsum1h9l
PubMed11358514
UniProtP00772|CELA1_PIG Chymotrypsin-like elastase family member 1 (Gene Name=CELA1)

[Back to BioLiP]