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Structure of monoclinic lysozyme obtained by multi crystal data collection

Analyse Structure of monoclinic lysozyme obtained by multi crystal data collection in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5A3Z
Type: protein
Length: 258 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Lysozyme
EC: 3.2.1.17
UniProt: B8YK79
Ligands: NO3
Pockets: 3 · best druggability 0.56

Structure

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

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Lysozyme (EC 3.2.1.17)	protein	129	41% helix, 11% strand	B8YK79

Ligands and binding sites

NO3 · Nitrate ion · ion · 2 copies · chains A, B
GOL · Glycerol · additive · chains B

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

Pockets

3 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	279	0.56	0.77	33	empty
2	67	0.32	0.75	17	empty
3	57	0.31	0.76	16	empty

Interfaces

1 interface between chains.

A–B · 196 Å² buried · 1 hydrogen bond · protein-protein

Modifications

Observed in the structure: 8 disulfide (disulfide).

Compared structures

5A3Z · Structure of monoclinic Lysozyme obtained by multi crystal data collection · 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 B8YK79
Elsewhere: RCSB PDB 5A3Z · PDBe 5A3Z · UniProt B8YK79

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