Structure of PDB 1lnb Chain E

Receptor sequence
>1lnbE (length=316) Species: 1427 (Bacillus thermoproteolyticus) [Search protein sequence]
ITGTSTVGVGRGVLGDQKNINTTYSTYYYLQDNTRGDGIFTYDAKYRTTL
PGSLWADADNQFFASYDAPAVDAHYYAGVTYDYYKNVHNRLSYDGNNAAI
RSSVHYSQGYNNAFWNGSEMVYGDGDGQTFIPLSGGIDVVAHELTHAVTD
YTAGLIYQNESGAINEAISDIFGTLVEFYANKNPDWEIGEDVYTPGISGD
SLRSMSDPAKYGDPDHYSKRYTGTQDNGGVHINSGIINKAAYLISQGGTH
YGVSVVGIGRDKLGKIFYRALTQYLTPTSNFSQLRAAAVQSATDLYGSTS
QEVASVKQAFDAVGVK
3D structure
PDB1lnb Structural analysis of zinc substitutions in the active site of thermolysin.
ChainE
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 VAL E N112 E143 R203 N112 E143 R203
BS02 FE E H142 H146 E166 H142 H146 E166
BS03 CA E D138 E177 D185 E187 E190 D138 E177 D185 E187 E190
BS04 CA E E177 N183 P184 D185 E190 E177 N183 P184 D185 E190
BS05 CA E D57 D59 Q61 D57 D59 Q61
BS06 CA E Y193 T194 I197 D200 Y193 T194 I197 D200
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
PDBsum1lnb
PubMed8535232
UniProtP00800|THER_BACTH Thermolysin (Gene Name=npr)

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