Structure of PDB 6lzo Chain A

Receptor sequence
>6lzoA (length=316) Species: 1427 (Bacillus thermoproteolyticus) [Search protein sequence]
ITGTSTVGVGRGVLGDQKNINTTYSTYYYLQDNTRGNGIFTYDAKYRTTL
PGSLWADADNQFFASYDAPAVDAHYYAGVTYDYYKNVHNRLSYDGNNAAI
RSSVHYSQGYNNAFWNGSQMVYGDGDGQTFIPLSGGIDVVAHELTHAVTD
YTAGLIYQNESGAINEAISDIFGTLVEFYANKNPDWEIGEDVYTPGISGD
SLRSMSDPAKYGDPDHYSKRYTGTQDNGGVHINSGIINKAAYLISQGGTH
YGVSVVGIGRDKLGKIFYRALTQYLTPTSNFSQLRAAAVQSATDLYGSTS
QEVASVKQAFDAVGVK
3D structure
PDB6lzo Structural analysis of metal chelation of the metalloproteinase thermolysin by 1,10-phenanthroline.
ChainA
Resolution1.8 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 3.4.24.27: thermolysin.
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 CA A Y193 T194 I197 D200 Y193 T194 I197 D200
BS02 CA A D138 E177 D185 E187 E190 D138 E177 D185 E187 E190
BS03 PHN A Y106 S107 Y110 Y106 S107 Y110 BindingDB: IC50=3.6nM
BS04 PHN A H216 S218 Y251 H216 S218 Y251 BindingDB: IC50=3.6nM
BS05 PHN A R11 Q17 Q61 F63 R11 Q17 Q61 F63 BindingDB: IC50=3.6nM
BS06 PHN A S5 N33 S5 N33 BindingDB: IC50=3.6nM
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:6lzo, PDBe:6lzo, PDBj:6lzo
PDBsum6lzo
PubMed33310458
UniProtP00800|THER_BACTH Thermolysin (Gene Name=npr)

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