Structure of PDB 1qf2 Chain A

Receptor sequence

>1qf2A (length=316) Species: 1427 (Bacillus thermoproteolyticus)

ITGTSTVGVGRGVLGDQKNINTTYSTYYYLQDNTRGDGIFTYDAKYRTTL
PGSLWADADNQFFASYDAPAVDAHYYAGVTYDYYKNVHNRLSYDGNNAAI
RSSVHYSQGYNNAFWNGSEMVYGDGDGQTFIPLSGGIDVVAHELTHAVTD
YTAGLIYQNESGAINEAISDIFGTLVEFYANKNPDWEIGEDVYTPGISGD
SLRSMSDPAKYGDPDHYSKRYTGTQDNGGVHINSGIINKAAYLISQGGTH
YGVSVVGIGRDKLGKIFYRALTQYLTPTSNFSQLRAAAVQSATDLYGSTS
QEVASVKQAFDAVGVK

3D structure

• PDB: 1qf2 Crystal structures of alpha-mercaptoacyldipeptides in the thermolysin active site: structural parameters for a Zn monodentation or bidentation in metalloendopeptidases.
• Chain: A
• Resolution: 2.06 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	A	H142 H146 E166	H142 H146 E166
BS02	CA	A	D138 E177 D185 E187 E190	D138 E177 D185 E187 E190
BS03	CA	A	E177 N183 D185 E190	E177 N183 D185 E190
BS04	CA	A	D57 D59 Q61	D57 D59 Q61
BS05	CA	A	Y193 T194 I197 D200	Y193 T194 I197 D200
BS06	TI3	A	N112 F130 L133 V139 H142 E143 L202 R203 H231	N112 F130 L133 V139 H142 E143 L202 R203 H231	MOAD: Ki=1200nM PDBbind-CN: -logKd/Ki=5.92,Ki=1200nM

Gene Ontology

Molecular Function

• GO:0004222 metalloendopeptidase activity

Biological Process

• GO:0006508 proteolysis

External links

• PDB: RCSB:1qf2, PDBe:1qf2, PDBj:1qf2
• PDBsum: 1qf2
• PubMed: 10504225
• UniProt: P00800|THER_BACTH Thermolysin (Gene Name=npr)