Structure of PDB 4oi5 Chain E

Receptor sequence

>4oi5E (length=316) Species: 1427 (Bacillus thermoproteolyticus)

ITGTSTVGVGRGVLGDQKNINTTYSTYYYLQDNTRGNGIFTYDAKYRTTL
PGSLWADADNQFFASYDAPAVDAHYYAGVTYDYYKNVHNRLSYDGNNAAI
RSSVHYSQGYNNAFWNGSQMVYGDGDGQTFIPLSGGIDVVAHELTHAVTD
YTAGLIYQNESGAINEAISDIFGTLVEFYANKNPDWEIGEDVYTPGISGD
SLRSMSDPAKYGDPDHYSKRYTGTQDNGGVHINSGIINKAAYLISQGGTH
YGVSVVGIGRDKLGKIFYRALTQYLTPTSNFSQLRAAAVQSATDLYGSTS
QEVASVKQAFDAVGVK

3D structure

• PDB: 4oi5 Methyl, Ethyl, Propyl, Butyl: Futile But Not for Water, as the Correlation of Structure and Thermodynamic Signature Shows in a Congeneric Series of Thermolysin Inhibitors.
• Chain: E
• Resolution: 1.3 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	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	E177 N183 D185 E190	E177 N183 D185 E190
BS05	CA	E	Y193 T194 I197 D200	Y193 T194 I197 D200
BS06	2G6	E	N112 A113 W115 N116 E143 H146 Y157 E166 L202 R203 H231	N112 A113 W115 N116 E143 H146 Y157 E166 L202 R203 H231

Gene Ontology

Molecular Function

• GO:0004222 metalloendopeptidase activity

Biological Process

• GO:0006508 proteolysis

External links

• PDB: RCSB:4oi5, PDBe:4oi5, PDBj:4oi5
• PDBsum: 4oi5
• PubMed: 24623396
• UniProt: P00800|THER_BACTH Thermolysin (Gene Name=npr)