Structure of PDB 1tmn Chain E

Receptor sequence
>1tmnE (length=316) Species: 1427 (Bacillus thermoproteolyticus) [Search protein sequence]
ITGTSTVGVGRGVLGDQKNINTTYSTYYYLQDNTRGDGIFTYDAKYRTTL
PGSLWADADNQFFASYDAPAVDAHYYAGVTYDYYKNVHNRLSYDGNNAAI
RSSVHYSQGYNNAFWNGSEMVYGDGDGQTFIPLSGGIDVVAHELTHAVTD
YTAGLIYQNESGAINEAISDIFGTLVEFYANKNPDWEIGEDVYTPGISGD
SLRSMSDPAKYGDPDHYSKRYTGTQDNGGVHINSGIINKAAYLISQGGTH
YGVSVVGIGRDKLGKIFYRALTQYLTPTSNFSQLRAAAVQSATDLYGSTS
QEVASVKQAFDAVGVK
3D structure
PDB1tmn Binding of N-carboxymethyl dipeptide inhibitors to thermolysin determined by X-ray crystallography: a novel class of transition-state analogues for zinc peptidases
ChainE
Resolution1.9 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 0ZN E Y110 N112 A113 H142 E143 H146 E166 L202 R203 H231 Y110 N112 A113 H142 E143 H146 E166 L202 R203 H231 MOAD: Ki=50nM
PDBbind-CN: -logKd/Ki=7.30,Ki=50nM
BS02 CA E D138 E177 D185 E187 E190 D138 E177 D185 E187 E190
BS03 CA E E177 N183 D185 E190 E177 N183 D185 E190
BS04 CA E D57 D59 Q61 D57 D59 Q61
BS05 CA E Y193 T194 I197 D200 Y193 T194 I197 D200
BS06 ZN E H142 H146 E166 H142 H146 E166
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:1tmn, PDBe:1tmn, PDBj:1tmn
PDBsum1tmn
PubMed6395881
UniProtP00800|THER_BACTH Thermolysin (Gene Name=npr)

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