Structure of PDB 3f2p Chain A

Receptor sequence
>3f2pA (length=316) Species: 1427 (Bacillus thermoproteolyticus) [Search protein sequence]
ITGTSTVGVGRGVLGDQKNINTTYSTYYYLQDNTRGDGIFTYDAKYRTTL
PGSLWADADNQFFASYDAPAVDAHYYAGVTYDYYKNVHNRLSYDGNNAAI
RSSVHYSQGYNNAFWNGSEMVYGDGDGQTFIPLSGGIDVVAHELTHAVTD
YTAGLIYQNESGAINEAISDIFGTLVEFYANKNPDWEIGEDVYTPGISGD
SLRSMSDPAKYGDPDHYSKRYTGTQDNGGVHINSGIINKAAYLISQGGTH
YGVSVVGIGRDKLGKIFYRALTQYLTPTSNFSQLRAAAVQSATDLYGSTS
QEVASVKQAFDAVGVK
3D structure
PDB3f2p Fragment-Based Lead Discovery: Screening and Optimizing Fragments for Thermolysin Inhibition.
ChainA
Resolution1.95 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 CA A D138 E177 D185 E187 E190 D138 E177 D185 E187 E190
BS02 CA A D57 D59 Q61 D57 D59 Q61
BS03 CA A Y193 T194 I197 D200 Y193 T194 I197 D200
BS04 ZN A H142 H146 E166 H142 H146 E166
BS05 S3B A N112 A113 V139 H142 E143 E166 R203 H231 N112 A113 V139 H142 E143 E166 R203 H231
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:3f2p, PDBe:3f2p, PDBj:3f2p
PDBsum3f2p
PubMed20394106
UniProtP00800|THER_BACTH Thermolysin (Gene Name=npr)

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