Structure of PDB 1at3 Chain B Binding Site BS01
Receptor Information
>1at3 Chain B (length=217) Species:
10310
(Human alphaherpesvirus 2) [
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RAVPIYVAGFLALYDSGDPGELALDPDTVRAALPPENPLPINVDHRARCE
VGRVLAVVNDPRGPFFVGLIACVQLERVLETAASAAILSREERLLYLITN
YLPSVSLSTKPDRTLFAHVALCAIGRRLGTIVTYDTSLDAAIAPFRHLDP
ATREGVRREAAEAELALAGRTWAPGVEALTHTLLSTAVNNMMLRDRWSLV
AERRRQAGIAGHTYLQA
Ligand information
Ligand ID
DFP
InChI
InChI=1S/C6H15O3P/c1-5(2)8-10(7)9-6(3)4/h5-6,10H,1-4H3
InChIKey
BLKXLEPPVDUHBY-UHFFFAOYSA-N
SMILES
Software
SMILES
CACTVS 3.341
CC(C)O[PH](=O)OC(C)C
OpenEye OEToolkits 1.5.0
CC(C)OP(=O)OC(C)C
ACDLabs 10.04
O=P(OC(C)C)OC(C)C
Formula
C6 H15 O3 P
Name
DIISOPROPYL PHOSPHONATE
ChEMBL
DrugBank
DB04491
ZINC
ZINC000100018862
PDB chain
1at3 Chain B Residue 300 [
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Receptor-Ligand Complex Structure
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PDB
1at3
Active site cavity of herpesvirus proteases revealed by the crystal structure of herpes simplex virus protease/inhibitor complex.
Resolution
2.5 Å
Binding residue
(original residue number in PDB)
H61 S129 R156
Binding residue
(residue number reindexed from 1)
H45 S106 R126
Annotation score
1
Enzymatic activity
Catalytic site (original residue number in PDB)
H61 S129 S131 H148 R156 R157
Catalytic site (residue number reindexed from 1)
H45 S106 S108 H118 R126 R127
Enzyme Commision number
3.4.21.97
: assemblin.
Gene Ontology
Molecular Function
GO:0004252
serine-type endopeptidase activity
Biological Process
GO:0006508
proteolysis
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Molecular Function
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Biological Process
External links
PDB
RCSB:1at3
,
PDBe:1at3
,
PDBj:1at3
PDBsum
1at3
PubMed
9369473
UniProt
Q69527
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