Structure of PDB 1thl Chain A Binding Site BS06

Receptor Information
>1thl Chain A (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 ID0DB
InChIInChI=1S/C28H32N2O5/c31-25(32)20(13-12-19-8-2-1-3-9-19)17-28(14-6-7-15-28)27(35)30-24(26(33)34)16-21-18-29-23-11-5-4-10-22(21)23/h1-5,8-11,18,20,24,29H,6-7,12-17H2,(H,30,35)(H,31,32)(H,33,34)/t20-,24+/m1/s1
InChIKeyMPZIROHQGMKFGS-YKSBVNFPSA-N
SMILES
SoftwareSMILES
CACTVS 3.341OC(=O)[C@H](CCc1ccccc1)CC2(CCCC2)C(=O)N[C@@H](Cc3c[nH]c4ccccc34)C(O)=O
ACDLabs 10.04O=C(O)C(CCc1ccccc1)CC4(C(=O)NC(C(=O)O)Cc3c2ccccc2nc3)CCCC4
CACTVS 3.341OC(=O)[CH](CCc1ccccc1)CC2(CCCC2)C(=O)N[CH](Cc3c[nH]c4ccccc34)C(O)=O
FormulaC28 H32 N2 O5
NameN-({1-[(2S)-2-carboxy-4-phenylbutyl]cyclopentyl}carbonyl)-L-tryptophan;
CCT
ChEMBL
DrugBank
ZINC
PDB chain1thl Chain A Residue 320 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1thl Inhibition of Thermolysin and Neutral Endopeptidase 24.11 By a Novel Glutaramide Derivative; X-Ray Structure Determination of the Thermolysin-Inhibitor Complex
Resolution1.7 Å
Binding residue
(original residue number in PDB)		N111 N112 A113 F130 V139 H142 E143 H146 E166 R203 H231
Binding residue
(residue number reindexed from 1)		N111 N112 A113 F130 V139 H142 E143 H146 E166 R203 H231
Annotation score1
Binding affinityMOAD: Ki=0.38uM
PDBbind-CN: -logKd/Ki=6.42,Ki=0.38uM
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.
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:1thl, PDBe:1thl, PDBj:1thl
PDBsum1thl
PubMed8286362
UniProtP00800|THER_BACTH Thermolysin (Gene Name=npr)

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