Structure of PDB 1os0 Chain A Binding Site BS06

Receptor Information
>1os0 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 ID0PQ
InChIInChI=1S/C27H31N2O5P/c28-25(18-22-14-8-3-9-15-22)35(33,34)19-23(16-20-10-4-1-5-11-20)26(30)29-24(27(31)32)17-21-12-6-2-7-13-21/h1-15,23-25H,16-19,28H2,(H,29,30)(H,31,32)(H,33,34)/t23-,24+,25-/m1/s1
InChIKeyXNPYGVCNHOXQRJ-DSNGMDLFSA-N
SMILES
SoftwareSMILES
CACTVS 3.370N[CH](Cc1ccccc1)[P](O)(=O)C[CH](Cc2ccccc2)C(=O)N[CH](Cc3ccccc3)C(O)=O
ACDLabs 12.01O=C(O)C(NC(=O)C(Cc1ccccc1)CP(=O)(O)C(N)Cc2ccccc2)Cc3ccccc3
CACTVS 3.370N[C@@H](Cc1ccccc1)[P](O)(=O)C[C@@H](Cc2ccccc2)C(=O)N[C@@H](Cc3ccccc3)C(O)=O
OpenEye OEToolkits 1.7.0c1ccc(cc1)CC(CP(=O)(C(Cc2ccccc2)N)O)C(=O)NC(Cc3ccccc3)C(=O)O
OpenEye OEToolkits 1.7.0c1ccc(cc1)C[C@H](C[P@@](=O)([C@H](Cc2ccccc2)N)O)C(=O)N[C@@H](Cc3ccccc3)C(=O)O
FormulaC27 H31 N2 O5 P
NameN-{(2R)-3-[(S)-[(1R)-1-amino-2-phenylethyl](hydroxy)phosphoryl]-2-benzylpropanoyl}-L-phenylalanine
ChEMBL
DrugBank
ZINCZINC000013807080
PDB chain1os0 Chain A Residue 605 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB1os0 Interactions of a new alpha-aminophosphinic derivative inside the active site of TLN (thermolysin): a model for zinc-metalloendopeptidase inhibition.
Resolution2.1 Å
Binding residue
(original residue number in PDB)		N112 A113 F114 V139 H142 E143 H146 E166 I188 L202 R203 H231
Binding residue
(residue number reindexed from 1)		N112 A113 F114 V139 H142 E143 H146 E166 I188 L202 R203 H231
Annotation score1
Binding affinityMOAD: Ki=0.93uM
PDBbind-CN: -logKd/Ki=6.03,Ki=0.93uM
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:1os0, PDBe:1os0, PDBj:1os0
PDBsum1os0
PubMed12832763
UniProtP00800|THER_BACTH Thermolysin (Gene Name=npr)

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