MolNFT v1 · #189456 · protein

Hen egg lysozyme refolded after denaturation at acidic pH

7VGP · Lysozyme C: “Hen egg lysozyme refolded after denaturation at acidic pH”. X-ray diffraction, 1 ligand (NA), 2 pockets (best druggability 0.61). MolNFT v1 #189456 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 7VGP
Type: protein
Length: 257 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Lysozyme C
EC: 3.2.1.17
UniProt: P00698
Ligands: NA
Pockets: 2 · best druggability 0.61

Structure

x-ray diffraction · 2 distinct chains · 41% helix, 11% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Lysozyme C (EC 3.2.1.17)	protein	129	41% helix, 11% strand	P00698
B	Lysozyme C (EC 3.2.1.17)	protein	128	41% helix, 11% strand	P00698

Ligands and binding sites

NA · Sodium ion · metal · 2 copies · chains A, B

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

Pockets

2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	380	0.61	0.77	40	empty
2	56	0.31	0.75	15	empty

Interfaces

1 interface between chains.

A–B · 288 Å² buried · 2 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 8 disulfide (disulfide).

Compared structures

7VGP · Hen egg lysozyme refolded after denaturation at acidic pH · the same entry in another collection · chain A against A, TM-score 1.00

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 7VGP · PDBe 7VGP · UniProt P00698

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