Structure of PDB 4owb Chain A

Receptor sequence
>4owbA (length=129) Species: 9031 (Gallus gallus) [Search protein sequence]
KVFGRCELAAAMKRHGLDNYRGYSLGNWVCAAKFESNFNTQATNRNTDGS
TDYGILQINSRWWCNDGRTPGSRNLCNIPCSALLSSDITASVNCAKKIVS
DGNGMNAWVAWRNRCKGTDVQAWIRGCRL
3D structure
PDB4owb Chemical conversion of cisplatin and carboplatin with histidine in a model protein crystallized under sodium iodide conditions.
ChainA
Resolution1.69 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 NA A S60 C64 N65 S72 R73 N74 S60 C64 N65 S72 R73 N74
BS02 BR A S24 G26 S24 G26
BS03 BR A G67 T69 G67 T69
BS04 BR A H15 T89 V92 H15 T89 V92
BS05 BR A C6 R128 C6 R128
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:4owb, PDBe:4owb, PDBj:4owb
PDBsum4owb
PubMed25195879
UniProtP00698|LYSC_CHICK Lysozyme C (Gene Name=LYZ)

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