Structure of PDB 1fju Chain A Binding Site BS03
Receptor Information
>1fju Chain A (length=316) Species:
1427
(Bacillus thermoproteolyticus) [
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ITGTSTVGVGRGVLGDQKNINTTYSTYYYLQDNTRGDGIFTYDAKYRTTL
PGSLWADADNQFFASYDAPAVDAHYYAGVTYDYYKNVHNRLSYDGNNAAI
RSSVHYSQGYNNAFWNGSEMVYGDGDGQTFIPLSGGIDVVAHELTHAVTD
YTAGLIYQNESGAINEAISDIFGTLVEFYANKNPDWEIGEDVYTPGISGD
SLRSMSDPAKYGDPDHYSKRYTGTQDNGGVHINSGIINKAAYLISQGGTH
YGVSVVGIGRDKLGKIFYRALTQYLTPTSNFSQLRAAAVQSATDLYGSTS
QEVASVKQAFDAVGVK
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
1fju Chain A Residue 503 [
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Receptor-Ligand Complex Structure
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PDB
1fju
Experimental and computational mapping of the binding surface of a crystalline protein.
Resolution
2.0 Å
Binding residue
(original residue number in PDB)
E177 N183 D185 E190
Binding residue
(residue number reindexed from 1)
E177 N183 D185 E190
Annotation score
4
Enzymatic activity
Catalytic site (original residue number in PDB)
H142 E143 H146 Y157 E166 D226 H231
Catalytic site (residue number reindexed from 1)
H142 E143 H146 Y157 E166 D226 H231
Enzyme Commision number
3.4.24.27
: thermolysin.
Gene Ontology
Molecular Function
GO:0004222
metalloendopeptidase activity
Biological Process
GO:0006508
proteolysis
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Molecular Function
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Biological Process
External links
PDB
RCSB:1fju
,
PDBe:1fju
,
PDBj:1fju
PDBsum
1fju
PubMed
11287678
UniProt
P00800
|THER_BACTH Thermolysin (Gene Name=npr)
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