Structure of PDB 3a94 Chain A

Receptor sequence
>3a94A (length=129) Species: 9031 (Gallus gallus) [Search protein sequence]
KVFGRCELAAAMKRHGLDNYRGYSLGNWVCAAKFESNFNTQATNRNTDGS
TDYGILQINSRWWCNDGRTPGSRNLCNIPCSALLSSDITASVNCAKKIVS
DGNGMNAWVAWRNRCKGTDVQAWIRGCRL
3D structure
PDB3a94 Elucidation of Metal-Ion Accumulation Induced by Hydrogen Bonds on Protein Surfaces by Using Porous Lysozyme Crystals Containing Rh(III) Ions as the Model Surfaces
ChainA
Resolution1.55 Å
3D
structure
Catalytic site residues are labeled in the structure
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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.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 RH3 A R14 H15 D87 R14 H15 D87
BS02 RH3 A N46 D52 N46 D52
BS03 RH3 A D18 N19 D18 N19
BS04 RH3 A R14 H15 R14 H15
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:3a94, PDBe:3a94, PDBj:3a94
PDBsum3a94
PubMed20146274
UniProtP00698|LYSC_CHICK Lysozyme C (Gene Name=LYZ)

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