MolNFT v2 · #216635 · protein

X-ray structure of the adduct formed upon reaction of Lysozyme with [Ru2Cl(DAniF)(O2CCH3)3] in condition A

8PFV · Lysozyme C: “X-ray structure of the adduct formed upon reaction of Lysozyme with [Ru2Cl(DAniF)(O2CCH3)3] in condition A”. X-ray diffraction at 1.46, 4 ligands (YMQ, NA, NO3), 1 pocket (best druggability 0.34). MolNFT v2 #216635 on…

PDB: 8PFV
Type: protein
Length: 129 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 1.46
Source: Gallus gallus
Molecule: Lysozyme C
EC: 3.2.1.17
UniProt: P00698
Ligands: YMQ, NA, NO3, CL
Pockets: 1 · best druggability 0.34

Structure

x-ray diffraction · resolution 1.46 · 1 distinct chain · 41% helix, 12% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
AAA	Lysozyme C (EC 3.2.1.17)	protein	129	41% helix, 12% strand	P00698

Ligands and binding sites

YMQ · 9,11-bis(4-methoxyphenyl)-3,7-dimethyl-2,4,6,8-tetraoxa-9,11-diaza-1$l^{4},5$l^{4}-diruthenatricyclo[3.3.3.0^{1,5}]undecane · ligand · chains AAA
NA · Sodium ion · metal · chains AAA
NO3 · Nitrate ion · ion · 5 copies · chains AAA
CL · Chloride ion · ion · chains AAA

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	75	0.34	0.75	14	NO3

Modifications

Observed in the structure: 4 disulfide (disulfide).

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt P00698
Elsewhere: RCSB PDB 8PFV · PDBe 8PFV · UniProt P00698

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