Structure of PDB 5js3 Chain E Binding Site BS06

Receptor Information
>5js3 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]
ITGTSTVGVGRGVLGDQKNINTTYSTYYYLQDNTRGNGIFTYDAKYRTTL
PGSLWADADNQFFASYDAPAVDAHYYAGVTYDYYKNVHNRLSYDGNNAAI
RSSVHYSQGYNNAFWNGSQMVYGDGDGQTFIPLSGGIDVVAHELTHAVTD
YTAGLIYQNESGAINEAISDIFGTLVEFYANKNPDWEIGEDVYTPGISGD
SLRSMSDPAKYGDPDHYSKRYTGTQDNGGVHINSGIINKAAYLISQGGTH
YGVSVVGIGRDKLGKIFYRALTQYLTPTSNFSQLRAAAVQSATDLYGSTS
QEVASVKQAFDAVGVK
Ligand information
Ligand ID6MG
InChIInChI=1S/C22H38N3O5P/c1-16(2)12-19(20(26)23-13-17(3)22(4,5)6)25-31(28,29)15-24-21(27)30-14-18-10-8-7-9-11-18/h7-11,16-17,19H,12-15H2,1-6H3,(H,23,26)(H,24,27)(H2,25,28,29)/t17-,19+/m1/s1
InChIKeyXXIXMIAOXNBYOY-MJGOQNOKSA-N
SMILES
SoftwareSMILES
ACDLabs 12.01C(CC(C)C)(C(=O)NCC(C(C)(C)C)C)NP(=O)(CNC(=O)OCc1ccccc1)O
OpenEye OEToolkits 2.0.4C[C@H](CNC(=O)[C@H](CC(C)C)NP(=O)(CNC(=O)OCc1ccccc1)O)C(C)(C)C
OpenEye OEToolkits 2.0.4CC(C)CC(C(=O)NCC(C)C(C)(C)C)NP(=O)(CNC(=O)OCc1ccccc1)O
CACTVS 3.385CC(C)C[CH](N[P](O)(=O)CNC(=O)OCc1ccccc1)C(=O)NC[CH](C)C(C)(C)C
CACTVS 3.385CC(C)C[C@H](N[P](O)(=O)CNC(=O)OCc1ccccc1)C(=O)NC[C@@H](C)C(C)(C)C
FormulaC22 H38 N3 O5 P
NameN~2~-[(R)-({[(benzyloxy)carbonyl]amino}methyl)(hydroxy)phosphoryl]-N-[(2S)-2,3,3-trimethylbutyl]-L-leucinamide
ChEMBL
DrugBank
ZINCZINC000584904946
PDB chain5js3 Chain E Residue 411 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB5js3 Rational Design of Thermodynamic and Kinetic Binding Profiles by Optimizing Surface Water Networks Coating Protein-Bound Ligands.
Resolution1.16 Å
Binding residue
(original residue number in PDB)		N112 A113 H142 E143 H146 Y157 E166 L202 R203 H231
Binding residue
(residue number reindexed from 1)		N112 A113 H142 E143 H146 Y157 E166 L202 R203 H231
Annotation score1
Binding affinityMOAD: Kd=0.185uM
PDBbind-CN: -logKd/Ki=6.73,Kd=0.185uM
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:5js3, PDBe:5js3, PDBj:5js3
PDBsum5js3
PubMed27933956
UniProtP00800|THER_BACTH Thermolysin (Gene Name=npr)

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