Structure of PDB 3fv4 Chain A Binding Site BS06

Receptor Information
>3fv4 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]
ITGTSTVGVGRGVLGDQKNINTTYSTYYYLQDNTRGNGIFTYDAKYRTTL
PGSLWADADNQFFASYDAPAVDAHYYAGVTYDYYKNVHNRLSYDGNNAAI
RSSVHYSQGYNNAFWNGSQMVYGDGDGQTFIPLSGGIDVVAHELTHAVTD
YTAGLIYQNESGAINEAISDIFGTLVEFYANKNPDWEIGEDVYTPGISGD
SLRSMSDPAKYGDPDHYSKRYTGTQDNGGVHINSGIINKAAYLISQGGTH
YGVSVVGIGRDKLGKIFYRALTQYLTPTSNFSQLRAAAVQSATDLYGSTS
QEVASVKQAFDAVGVK
Ligand information
Ligand ID1U4
InChIInChI=1S/C24H32N3O7P/c1-17(2)13-21(23(29)30)26-22(28)20(14-18-9-5-3-6-10-18)27-35(32,33)16-25-24(31)34-15-19-11-7-4-8-12-19/h3-12,17,20-21H,13-16H2,1-2H3,(H,25,31)(H,26,28)(H,29,30)(H2,27,32,33)/t20-,21-/m0/s1
InChIKeyXQFJAKNVSJXHDS-SFTDATJTSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.7.0CC(C)CC(C(=O)O)NC(=O)C(Cc1ccccc1)NP(=O)(CNC(=O)OCc2ccccc2)O
OpenEye OEToolkits 1.7.0CC(C)C[C@@H](C(=O)O)NC(=O)[C@H](Cc1ccccc1)N[P@](=O)(CNC(=O)OCc2ccccc2)O
ACDLabs 12.01O=C(O)C(NC(=O)C(NP(=O)(O)CNC(=O)OCc1ccccc1)Cc2ccccc2)CC(C)C
CACTVS 3.370CC(C)C[C@H](NC(=O)[C@H](Cc1ccccc1)N[P](O)(=O)CNC(=O)OCc2ccccc2)C(O)=O
CACTVS 3.370CC(C)C[CH](NC(=O)[CH](Cc1ccccc1)N[P](O)(=O)CNC(=O)OCc2ccccc2)C(O)=O
FormulaC24 H32 N3 O7 P
NameN-[(S)-({[(benzyloxy)carbonyl]amino}methyl)(hydroxy)phosphoryl]-L-phenylalanyl-L-leucine
ChEMBL
DrugBank
ZINCZINC000058632085
PDB chain3fv4 Chain A 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]
PDB3fv4 Displacement of disordered water molecules from hydrophobic pocket creates enthalpic signature: binding of phosphonamidate to the S1'-pocket of thermolysin.
Resolution1.56 Å
Binding residue
(original residue number in PDB)		N112 A113 F114 W115 F130 V139 H142 E143 H146 Y157 E166 I188 L202 R203 H231
Binding residue
(residue number reindexed from 1)		N112 A113 F114 W115 F130 V139 H142 E143 H146 Y157 E166 I188 L202 R203 H231
Annotation score1
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:3fv4, PDBe:3fv4, PDBj:3fv4
PDBsum3fv4
PubMed20600625
UniProtP00800|THER_BACTH Thermolysin (Gene Name=npr)

[Back to BioLiP]