Structure of PDB 5lvd Chain E

Receptor sequence
>5lvdE (length=316) Species: 1427 (Bacillus thermoproteolyticus) [Search protein sequence]
ITGTSTVGVGRGVLGDQKNINTTYSTYYYLQDNTRGNGIFTYDAKYRTTL
PGSLWADADNQFFASYDAPAVDAHYYAGVTYDYYKNVHNRLSYDGNNAAI
RSSVHYSQGYNNAFWNGSQMVYGDGDGQTFIPLSGGIDVVAHELTHAVTD
YTAGLIYQNESGAINEAISDIFGTLVEFYANKNPDWEIGEDVYTPGISGD
SLRSMSDPAKYGDPDHYSKRYTGTQDNGGVHINSGIINKAAYLISQGGTH
YGVSVVGIGRDKLGKIFYRALTQYLTPTSNFSQLRAAAVQSATDLYGSTS
QEVASVKQAFDAVGVK
3D structure
PDB5lvd How Nothing Boosts Affinity: Hydrophobic Ligand Binding to the Virtually Vacated S1' Pocket of Thermolysin.
ChainE
Resolution1.25 Å
3D
structure
Catalytic site residues are labeled in the structure
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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.
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 ZN E H142 H146 E166 H142 H146 E166
BS02 CA E D138 E177 D185 E187 E190 D138 E177 D185 E187 E190
BS03 CA E D57 D59 Q61 D57 D59 Q61
BS04 CA E Y193 T194 I197 D200 Y193 T194 I197 D200
BS05 CA E E177 N183 D185 E190 E177 N183 D185 E190
BS06 79F E N112 A113 E143 H146 E166 R203 H231 N112 A113 E143 H146 E166 R203 H231 MOAD: Kd=2.4mM
PDBbind-CN: -logKd/Ki=2.62,Kd=2.4mM
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:5lvd, PDBe:5lvd, PDBj:5lvd
PDBsum5lvd
PubMed28696673
UniProtP00800|THER_BACTH Thermolysin (Gene Name=npr)

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