Structure of PDB 1tmn Chain E Binding Site BS01

Receptor Information
>1tmn Chain E (length=316) Species: 1427 (Bacillus thermoproteolyticus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
ITGTSTVGVGRGVLGDQKNINTTYSTYYYLQDNTRGDGIFTYDAKYRTTL
PGSLWADADNQFFASYDAPAVDAHYYAGVTYDYYKNVHNRLSYDGNNAAI
RSSVHYSQGYNNAFWNGSEMVYGDGDGQTFIPLSGGIDVVAHELTHAVTD
YTAGLIYQNESGAINEAISDIFGTLVEFYANKNPDWEIGEDVYTPGISGD
SLRSMSDPAKYGDPDHYSKRYTGTQDNGGVHINSGIINKAAYLISQGGTH
YGVSVVGIGRDKLGKIFYRALTQYLTPTSNFSQLRAAAVQSATDLYGSTS
QEVASVKQAFDAVGVK
Ligand information
Ligand ID0ZN
InChIInChI=1S/C27H33N3O5/c1-17(2)14-23(29-22(26(32)33)13-12-18-8-4-3-5-9-18)25(31)30-24(27(34)35)15-19-16-28-21-11-7-6-10-20(19)21/h3-11,16-17,22-24,28-29H,12-15H2,1-2H3,(H,30,31)(H,32,33)(H,34,35)/t22-,23-,24-/m0/s1
InChIKeyPAPCSVADGJFRFM-HJOGWXRNSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0CC(C)CC(C(=O)NC(Cc1c[nH]c2c1cccc2)C(=O)O)NC(CCc3ccccc3)C(=O)O
CACTVS 3.341CC(C)C[C@H](N[C@@H](CCc1ccccc1)C(O)=O)C(=O)N[C@@H](Cc2c[nH]c3ccccc23)C(O)=O
ACDLabs 10.04O=C(O)C(NC(C(=O)NC(C(=O)O)Cc2c1ccccc1nc2)CC(C)C)CCc3ccccc3
OpenEye OEToolkits 1.5.0CC(C)C[C@@H](C(=O)N[C@@H](Cc1c[nH]c2c1cccc2)C(=O)O)N[C@@H](CCc3ccccc3)C(=O)O
CACTVS 3.341CC(C)C[CH](N[CH](CCc1ccccc1)C(O)=O)C(=O)N[CH](Cc2c[nH]c3ccccc23)C(O)=O
FormulaC27 H33 N3 O5
NameN-[(1R)-1-carboxy-3-phenylpropyl]-L-leucyl-L-tryptophan
ChEMBL
DrugBank
ZINCZINC000026665926
PDB chain1tmn Chain E Residue 317 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB1tmn Binding of N-carboxymethyl dipeptide inhibitors to thermolysin determined by X-ray crystallography: a novel class of transition-state analogues for zinc peptidases
Resolution1.9 Å
Binding residue
(original residue number in PDB)		Y110 N112 A113 H142 E143 H146 E166 L202 R203 H231
Binding residue
(residue number reindexed from 1)		Y110 N112 A113 H142 E143 H146 E166 L202 R203 H231
Annotation score1
Binding affinityMOAD: Ki=50nM
PDBbind-CN: -logKd/Ki=7.30,Ki=50nM
Enzymatic activity
Enzyme Commision number 3.4.24.27: thermolysin.
Gene Ontology
Molecular Function
GO:0004222 metalloendopeptidase activity
Biological Process
GO:0006508 proteolysis

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:1tmn, PDBe:1tmn, PDBj:1tmn
PDBsum1tmn
PubMed6395881
UniProtP00800|THER_BACTH Thermolysin (Gene Name=npr)

[Back to BioLiP]