Structure of PDB 5i54 Chain A

Receptor sequence

>5i54A (length=129) Species: 9031 (Gallus gallus)

KVFGRCELAAAMKRHGLDNYRGYSLGNWVCAAKFESNFNTQATNRNTDGS
TDYGILQINSRWWCNDGRTPGSRNLCNIPCSALLSSDITASVNCAKKIVS
DGNGMNAWVAWRNRCKGTDVQAWIRGCRL

3D structure

• PDB: 5i54 Time-dependent X-ray diffraction studies on urea/hen egg white lysozyme complexes reveal structural changes that indicate onset of denaturation
• Chain: A
• Resolution: 1.608 Å

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	URE	A	A10 R14	A10 R14
BS02	URE	A	T43 R45	T43 R45
BS03	URE	A	C6 R128	C6 R128
BS04	URE	A	C127 L129	C127 L129
BS05	URE	A	G67 T69 S72	G67 T69 S72
BS06	URE	A	N59 A107 W108	N59 A107 W108

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

External links

• PDB: RCSB:5i54, PDBe:5i54, PDBj:5i54
• PDBsum: 5i54
• PubMed: 27573790
• UniProt: P00698|LYSC_CHICK Lysozyme C (Gene Name=LYZ)