Structure of PDB 5dpe Chain E

Receptor sequence

>5dpeE (length=316) Species: 1427 (Bacillus thermoproteolyticus)

ITGTSTVGVGRGVLGDQKNINTTYSTYYYLQDNTRGNGIFTYDAKYRTTL
PGSLWADADNQFFASYDAPAVDAHYYAGVTYDYYKNVHNRLSYDGNNAAI
RSSVHYSQGYNNAFWNGSQMVYGDGDGQTFIPLSGGIDVVAHELTHAVTD
YTAGLIYQNESGAINEAISDIFGTLVEFYANKNPDWEIGEDVYTPGISGD
SLRSMSDPAKYGDPDHYSKRYTGTQDNGGVHINSGIINKAAYLISQGGTH
YGVSVVGIGRDKLGKIFYRALTQYLTPTSNFSQLRAAAVQSATDLYGSTS
QEVASVKQAFDAVGVK

3D structure

• PDB: 5dpe Thermodynamics of protein-ligand interactions as a reference for computational analysis: how to assess accuracy, reliability and relevance of experimental data.
• Chain: E
• Resolution: 1.34 Å

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	5H8	E	N112 A113 W115 H142 E143 H146 Y157 E166 L202 R203 H231	N112 A113 W115 H142 E143 H146 Y157 E166 L202 R203 H231
BS02	ZN	E	H142 H146 E166	H142 H146 E166
BS03	CA	E	D138 E177 D185 E187 E190	D138 E177 D185 E187 E190
BS04	CA	E	D57 D59 Q61	D57 D59 Q61
BS05	CA	E	E177 N183 D185 E190	E177 N183 D185 E190
BS06	CA	E	Y193 T194 I197 D200	Y193 T194 I197 D200

Gene Ontology

Molecular Function

• GO:0004222 metalloendopeptidase activity

Biological Process

• GO:0006508 proteolysis

External links

• PDB: RCSB:5dpe, PDBe:5dpe, PDBj:5dpe
• PDBsum: 5dpe
• PubMed: 26376645
• UniProt: P00800|THER_BACTH Thermolysin (Gene Name=npr)