Structure of PDB 183l Chain A Binding Site BS01
Receptor Information
>183l Chain A (length=162) Species:
10665
(Tequatrovirus T4) [
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MNIFEMLRIDEGLRLKIYKDTEGYYTIGIGHLLTKSPSLNAAKSELDKAI
GRNTNGVITKDEAEKLFNQDVDAAVRGILRNAKLKPVYDSLDAVRRAAAI
NMVFQMGETGVAGFTNSLRMLQQKRWDEAAVNLAKSRWYNQTPNRAKRVI
TTFRTGTWDAYK
Ligand information
Ligand ID
DEN
InChI
InChI=1S/C9H8/c1-2-5-9-7-3-6-8(9)4-1/h1-6H,7H2
InChIKey
YBYIRNPNPLQARY-UHFFFAOYSA-N
SMILES
Software
SMILES
CACTVS 3.341
C1C=Cc2ccccc12
OpenEye OEToolkits 1.5.0
c1ccc2c(c1)CC=C2
ACDLabs 10.04
c1cccc2c1C=CC2
Formula
C9 H8
Name
INDENE
ChEMBL
CHEMBL192812
DrugBank
ZINC
ZINC000001699888
PDB chain
183l Chain A Residue 400 [
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Receptor-Ligand Complex Structure
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PDB
183l
Specificity of ligand binding in a buried nonpolar cavity of T4 lysozyme: linkage of dynamics and structural plasticity.
Resolution
1.8 Å
Binding residue
(original residue number in PDB)
V87 Y88 A99 L118
Binding residue
(residue number reindexed from 1)
V87 Y88 A99 L118
Annotation score
1
Binding affinity
MOAD
: Ka=5170M^-1
Enzymatic activity
Catalytic site (original residue number in PDB)
E11 D20
Catalytic site (residue number reindexed from 1)
E11 D20
Enzyme Commision number
3.2.1.17
: lysozyme.
Gene Ontology
Molecular Function
GO:0003796
lysozyme activity
GO:0016798
hydrolase activity, acting on glycosyl bonds
Biological Process
GO:0009253
peptidoglycan catabolic process
GO:0016998
cell wall macromolecule catabolic process
GO:0031640
killing of cells of another organism
GO:0042742
defense response to bacterium
GO:0044659
viral release from host cell by cytolysis
Cellular Component
GO:0030430
host cell cytoplasm
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Molecular Function
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Biological Process
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Cellular Component
External links
PDB
RCSB:183l
,
PDBe:183l
,
PDBj:183l
PDBsum
183l
PubMed
7612599
UniProt
P00720
|ENLYS_BPT4 Endolysin (Gene Name=E)
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