Structure of PDB 1fjv Chain A Binding Site BS01
Receptor Information
>1fjv Chain A (length=316) Species:
1427
(Bacillus thermoproteolyticus) [
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ITGTSTVGVGRGVLGDQKNINTTYSTYYYLQDNTRGDGIFTYDAKYRTTL
PGSLWADADNQFFASYDAPAVDAHYYAGVTYDYYKNVHNRLSYDGNNAAI
RSSVHYSQGYNNAFWNGSEMVYGDGDGQTFIPLSGGIDVVAHELTHAVTD
YTAGLIYQNESGAINEAISDIFGTLVEFYANKNPDWEIGEDVYTPGISGD
SLRSMSDPAKYGDPDHYSKRYTGTQDNGGVHINSGIINKAAYLISQGGTH
YGVSVVGIGRDKLGKIFYRALTQYLTPTSNFSQLRAAAVQSATDLYGSTS
QEVASVKQAFDAVGVK
Ligand information
Ligand ID
ZN
InChI
InChI=1S/Zn/q+2
InChIKey
PTFCDOFLOPIGGS-UHFFFAOYSA-N
SMILES
Software
SMILES
CACTVS 3.341
[Zn++]
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Zn+2]
Formula
Zn
Name
ZINC ION
ChEMBL
CHEMBL1236970
DrugBank
DB14532
ZINC
PDB chain
1fjv Chain A Residue 501 [
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Receptor-Ligand Complex Structure
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PDB
1fjv
Experimental and computational mapping of the binding surface of a crystalline protein.
Resolution
2.0 Å
Binding residue
(original residue number in PDB)
H142 H146 E166
Binding residue
(residue number reindexed from 1)
H142 H146 E166
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:1fjv
,
PDBe:1fjv
,
PDBj:1fjv
PDBsum
1fjv
PubMed
11287678
UniProt
P00800
|THER_BACTH Thermolysin (Gene Name=npr)
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