Structure of PDB 6ro3 Chain A

Receptor sequence

>6ro3A (length=129) Species: 9031 (Gallus gallus)

KVFGRCELAAAMKRHGLDNYRGYSLGNWVCAAKFESNFNTQATNRNTDGS
TDYGILQINSRWWCNDGRTPGSRNLCNIPCSALLSSDITASVNCAKKIVS
DGNGMNAWVAWRNRCKGTDVQAWIRGCRL

3D structure

• PDB: 6ro3 Formation of a highly dense tetra-rhenium cluster in a protein crystal and its implications in medical imaging.
• Chain: A
• Resolution: 1.03 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	RE	A	K1 E7	K1 E7
BS02	KBW	A	D48 R61 T69 P70 G71 S72	D48 R61 T69 P70 G71 S72
BS03	KBW	A	R5 K33 W123	R5 K33 W123
BS04	KBW	A	G117 T118 D119	G117 T118 D119
BS05	RRE	A	A11 R14 H15 D87	A11 R14 H15 D87

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:6ro3, PDBe:6ro3, PDBj:6ro3
• PDBsum: 6ro3
• PubMed: 31316813
• UniProt: P00698|LYSC_CHICK Lysozyme C (Gene Name=LYZ)