Structure of PDB 1cse Chain E Binding Site BS02
Receptor Information
>1cse Chain E (length=274) Species:
1423
(Bacillus subtilis) [
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AQTVPYGIPLIKADKVQAQGFKGANVKVAVLDTGIQASHPDLNVVGGASF
VAGEAYNTDGNGHGTHVAGTVAALDNTTGVLGVAPSVSLYAVKVLNSSGS
GSYSGIVSGIEWATTNGMDVINMSLGGASGSTAMKQAVDNAYARGVVVVA
AAGNSGNSGSTNTIGYPAKYDSVIAVGAVDSNSNRASFSSVGAELEVMAP
GAGVYSTYPTNTYATLNGTSMASPHVAGAAALILSKHPNLSASQVRNRLS
STATYLGSSFYYGKGLINVEAAAQ
Ligand information
Ligand ID
CA
InChI
InChI=1S/Ca/q+2
InChIKey
BHPQYMZQTOCNFJ-UHFFFAOYSA-N
SMILES
Software
SMILES
CACTVS 3.341
[Ca++]
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Ca+2]
Formula
Ca
Name
CALCIUM ION
ChEMBL
DrugBank
DB14577
ZINC
PDB chain
1cse Chain E Residue 430 [
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Receptor-Ligand Complex Structure
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PDB
1cse
The high-resolution X-ray crystal structure of the complex formed between subtilisin Carlsberg and eglin c, an elastase inhibitor from the leech Hirudo medicinalis. Structural analysis, subtilisin structure and interface geometry.
Resolution
1.2 Å
Binding residue
(original residue number in PDB)
Q2 D41 L75 N77 T79 V81
Binding residue
(residue number reindexed from 1)
Q2 D41 L74 N76 T78 V80
Annotation score
4
Enzymatic activity
Catalytic site (original residue number in PDB)
S221
Catalytic site (residue number reindexed from 1)
S220
Enzyme Commision number
3.4.21.62
: subtilisin.
Gene Ontology
Molecular Function
GO:0004252
serine-type endopeptidase activity
GO:0008236
serine-type peptidase activity
Biological Process
GO:0006508
proteolysis
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Molecular Function
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Biological Process
External links
PDB
RCSB:1cse
,
PDBe:1cse
,
PDBj:1cse
PDBsum
1cse
PubMed
3301348
UniProt
B0FXJ2
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