MolNFT v2 · #228782 · protein

X-ray structure of lysozyme obtained upon reaction with the dioxidovanadium(V) complex with (E)-N'-(1-(2-hydroxy-5-methoxyphenyl)ethylidene)furan-2-carbohydrazide)

9GOK · Lysozyme C: “X-ray structure of lysozyme obtained upon reaction with the dioxidovanadium(V) complex with…”. X-ray diffraction at 1.18, 3 ligands (A1ION, NA, CL), 1 pocket (best druggability 0.34). MolNFT v2 #228782 on GenesisL1: 3D…

PDB: 9GOK
Type: protein
Length: 129 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 1.18
Source: Gallus gallus
Molecule: Lysozyme C
EC: 3.2.1.17
UniProt: P00698
Ligands: A1ION, NA, CL
Pockets: 1 · best druggability 0.34

Structure

x-ray diffraction · resolution 1.18 · 1 distinct chain · 41% helix, 11% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
AAA	Lysozyme C (EC 3.2.1.17)	protein	129	41% helix, 11% strand	P00698

Ligands and binding sites

A1ION · dioxidovanadium(V) complex with (E)-N'-(1-(2-hydroxy-5-methoxyphenyl)ethylidene)furan-2-carbohydrazide · ligand · 2 copies · chains AAA
NA · Sodium ion · metal · chains AAA
CL · Chloride ion · ion · 3 copies · chains AAA
ACT · Acetate ion · additive · 2 copies · 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	0.76	19	ACT

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 9GOK · PDBe 9GOK · UniProt P00698

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