Structure of PDB 2ybn Chain A Binding Site BS01
Receptor Information
>2ybn Chain A (length=129) Species:
9031
(Gallus gallus) [
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KVFGRCELAAAMKRHGLDNYRGYSLGNWVCAAKFESNFNTQATNRNTDGS
TDYGILQINSRWWCNDGRTPGSRNLCNIPCSALLSSDITASVNCAKKIVS
DGNGMNAWVAWRNRCKGTDVQAWIRGCRL
Ligand information
Ligand ID
NO2
InChI
InChI=1S/HNO2/c2-1-3/h(H,2,3)/p-1
InChIKey
IOVCWXUNBOPUCH-UHFFFAOYSA-M
SMILES
Software
SMILES
ACDLabs 10.04
CACTVS 3.341
[O-]N=O
OpenEye OEToolkits 1.5.0
N(=O)[O-]
Formula
N O2
Name
NITRITE ION
ChEMBL
DrugBank
DB12529
ZINC
PDB chain
2ybn Chain A Residue 1130 [
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Receptor-Ligand Complex Structure
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PDB
2ybn
Effective Scavenging at Cryotemperatures: Further Increasing the Dose Tolerance of Protein Crystals.
Resolution
2.0 Å
Binding residue
(original residue number in PDB)
N65 D66 G67 T69 S72
Binding residue
(residue number reindexed from 1)
N65 D66 G67 T69 S72
Annotation score
1
Enzymatic activity
Catalytic site (original residue number in PDB)
E35 N46 D48 S50 D52 N59
Catalytic site (residue number reindexed from 1)
E35 N46 D48 S50 D52 N59
Enzyme Commision number
3.2.1.17
: lysozyme.
Gene Ontology
Molecular Function
GO:0003796
lysozyme activity
GO:0005515
protein binding
GO:0016231
beta-N-acetylglucosaminidase activity
GO:0016798
hydrolase activity, acting on glycosyl bonds
GO:0042802
identical protein binding
Biological Process
GO:0016998
cell wall macromolecule catabolic process
GO:0031640
killing of cells of another organism
GO:0042742
defense response to bacterium
GO:0050829
defense response to Gram-negative bacterium
GO:0050830
defense response to Gram-positive bacterium
Cellular Component
GO:0005576
extracellular region
GO:0005615
extracellular space
GO:0005737
cytoplasm
GO:0005783
endoplasmic reticulum
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Molecular Function
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Biological Process
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Cellular Component
External links
PDB
RCSB:2ybn
,
PDBe:2ybn
,
PDBj:2ybn
PDBsum
2ybn
PubMed
21525642
UniProt
P00698
|LYSC_CHICK Lysozyme C (Gene Name=LYZ)
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