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Crystal structure of mutant human lysozyme substituted at the surface positions

Analyse Crystal structure of mutant human lysozyme substituted at the surface positions in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1GBY
Type: protein
Length: 130 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Lysozyme
EC: 3.2.1.17
UniProt: P61626
Ligands: NA
Pockets: 1 · best druggability 0.31

Structure

x-ray diffraction · 1 distinct chain · 39% helix, 12% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Lysozyme (EC 3.2.1.17)	protein	130	39% helix, 12% strand	P61626

Ligands and binding sites

NA · Sodium ion · metal

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	63	0.31	0.75	13	empty

Modifications

Observed in the structure: 4 disulfide (disulfide).

Compared structures

1GBY · Crystal structure of mutant human lysozyme substituted at the surface positions · 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 P61626
Elsewhere: RCSB PDB 1GBY · PDBe 1GBY · UniProt P61626

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