Structure of PDB 5n34 Chain E Binding Site BS06

Receptor Information
>5n34 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 ID8JQ
InChIInChI=1S/C17H29N4O5P/c1-13(2)10-15(16(22)19-9-8-18)21-27(24,25)12-20-17(23)26-11-14-6-4-3-5-7-14/h3-7,13,15H,8-12,18H2,1-2H3,(H,19,22)(H,20,23)(H2,21,24,25)/t15-/m0/s1
InChIKeyPVGHXKGUTYHASF-HNNXBMFYSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 2.0.6CC(C)C[C@@H](C(=O)NCCN)NP(=O)(CNC(=O)OCc1ccccc1)O
OpenEye OEToolkits 2.0.6CC(C)CC(C(=O)NCCN)NP(=O)(CNC(=O)OCc1ccccc1)O
CACTVS 3.385CC(C)C[C@H](N[P](O)(=O)CNC(=O)OCc1ccccc1)C(=O)NCCN
CACTVS 3.385CC(C)C[CH](N[P](O)(=O)CNC(=O)OCc1ccccc1)C(=O)NCCN
FormulaC17 H29 N4 O5 P
Name~{N}-[(2~{S})-1-(2-azanylethylamino)-4-methyl-1-oxidanylidene-pentan-2-yl]-(phenylmethoxycarbonylaminomethyl)phosphonamidic acid
ChEMBLCHEMBL4089068
DrugBank
ZINC
PDB chain5n34 Chain E Residue 412 [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]
PDB5n34 Paying the Price of Desolvation in Solvent-Exposed Protein Pockets: Impact of Distal Solubilizing Groups on Affinity and Binding Thermodynamics in a Series of Thermolysin Inhibitors.
Resolution1.22 Å
Binding residue
(original residue number in PDB)		N112 A113 F114 N116 E143 H146 Y157 E166 L202 R203 H231
Binding residue
(residue number reindexed from 1)		N112 A113 F114 N116 E143 H146 Y157 E166 L202 R203 H231
Annotation score1
Binding affinityPDBbind-CN: -logKd/Ki=4.63,Kd=23.27uM
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:5n34, PDBe:5n34, PDBj:5n34
PDBsum5n34
PubMed28590130
UniProtP00800|THER_BACTH Thermolysin (Gene Name=npr)

[Back to BioLiP]