Structure of PDB 2tmn Chain E Binding Site BS06

Receptor Information
>2tmn 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 ID0FA
InChIInChI=1S/C6H15N2O4P/c1-4(2)3-5(6(7)9)8-13(10,11)12/h4-5H,3H2,1-2H3,(H2,7,9)(H3,8,10,11,12)/t5-/m0/s1
InChIKeyLHNDGZQCKJAVRF-YFKPBYRVSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.7.0CC(C)CC(C(=O)N)NP(=O)(O)O
OpenEye OEToolkits 1.7.0CC(C)C[C@@H](C(=O)N)NP(=O)(O)O
CACTVS 3.370CC(C)C[CH](N[P](O)(O)=O)C(N)=O
CACTVS 3.370CC(C)C[C@H](N[P](O)(O)=O)C(N)=O
ACDLabs 12.01O=P(O)(O)NC(C(=O)N)CC(C)C
FormulaC6 H15 N2 O4 P
NameN~2~-phosphono-L-leucinamide
ChEMBLCHEMBL47541
DrugBank
ZINC
PDB chain2tmn Chain E Residue 322 [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]
PDB2tmn Crystallographic structural analysis of phosphoramidates as inhibitors and transition-state analogs of thermolysin.
Resolution1.6 Å
Binding residue
(original residue number in PDB)		N112 A113 E143 H146 E166 R203 H231
Binding residue
(residue number reindexed from 1)		N112 A113 E143 H146 E166 R203 H231
Annotation score1
Binding affinityMOAD: Ki=1.3uM
PDBbind-CN: -logKd/Ki=5.89,Ki=1.3uM
BindingDB: Ki=21300nM,Kd=1288nM
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:2tmn, PDBe:2tmn, PDBj:2tmn
PDBsum2tmn
PubMed3709536
UniProtP00800|THER_BACTH Thermolysin (Gene Name=npr)

[Back to BioLiP]