Structure of PDB 2tmn Chain E

Receptor sequence
>2tmnE (length=316) Species: 1427 (Bacillus thermoproteolyticus) [Search protein sequence]
ITGTSTVGVGRGVLGDQKNINTTYSTYYYLQDNTRGDGIFTYDAKYRTTL
PGSLWADADNQFFASYDAPAVDAHYYAGVTYDYYKNVHNRLSYDGNNAAI
RSSVHYSQGYNNAFWNGSEMVYGDGDGQTFIPLSGGIDVVAHELTHAVTD
YTAGLIYQNESGAINEAISDIFGTLVEFYANKNPDWEIGEDVYTPGISGD
SLRSMSDPAKYGDPDHYSKRYTGTQDNGGVHINSGIINKAAYLISQGGTH
YGVSVVGIGRDKLGKIFYRALTQYLTPTSNFSQLRAAAVQSATDLYGSTS
QEVASVKQAFDAVGVK
3D structure
PDB2tmn Crystallographic structural analysis of phosphoramidates as inhibitors and transition-state analogs of thermolysin.
ChainE
Resolution1.6 Å
3D
structure
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Enzymatic activity
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 E D138 E177 D185 E187 E190 D138 E177 D185 E187 E190
BS02 CA E E177 N183 D185 E190 E177 N183 D185 E190
BS03 CA E D57 D59 Q61 D57 D59 Q61
BS04 CA E Y193 T194 I197 D200 Y193 T194 I197 D200
BS05 ZN E H142 H146 E166 H142 H146 E166
BS06 0FA E N112 A113 E143 H146 E166 R203 H231 N112 A113 E143 H146 E166 R203 H231 MOAD: Ki=1.3uM
PDBbind-CN: -logKd/Ki=5.89,Ki=1.3uM
BindingDB: Ki=21300nM,Kd=1288nM
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:2tmn, PDBe:2tmn, PDBj:2tmn
PDBsum2tmn
PubMed3709536
UniProtP00800|THER_BACTH Thermolysin (Gene Name=npr)

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