Structure of PDB 1lnb Chain E Binding Site BS02
Receptor Information
>1lnb Chain E (length=316) Species:
1427
(Bacillus thermoproteolyticus) [
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ITGTSTVGVGRGVLGDQKNINTTYSTYYYLQDNTRGDGIFTYDAKYRTTL
PGSLWADADNQFFASYDAPAVDAHYYAGVTYDYYKNVHNRLSYDGNNAAI
RSSVHYSQGYNNAFWNGSEMVYGDGDGQTFIPLSGGIDVVAHELTHAVTD
YTAGLIYQNESGAINEAISDIFGTLVEFYANKNPDWEIGEDVYTPGISGD
SLRSMSDPAKYGDPDHYSKRYTGTQDNGGVHINSGIINKAAYLISQGGTH
YGVSVVGIGRDKLGKIFYRALTQYLTPTSNFSQLRAAAVQSATDLYGSTS
QEVASVKQAFDAVGVK
Ligand information
Ligand ID
FE
InChI
InChI=1S/Fe/q+3
InChIKey
VTLYFUHAOXGGBS-UHFFFAOYSA-N
SMILES
Software
SMILES
ACDLabs 10.04
CACTVS 3.341
OpenEye OEToolkits 1.5.0
[Fe+3]
Formula
Fe
Name
FE (III) ION
ChEMBL
DrugBank
DB13949
ZINC
PDB chain
1lnb Chain E Residue 900 [
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Receptor-Ligand Complex Structure
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PDB
1lnb
Structural analysis of zinc substitutions in the active site of thermolysin.
Resolution
1.8 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
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:1lnb
,
PDBe:1lnb
,
PDBj:1lnb
PDBsum
1lnb
PubMed
8535232
UniProt
P00800
|THER_BACTH Thermolysin (Gene Name=npr)
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