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Engineered beta-lactoglobulin: variant M107L

Analyse Engineered beta-lactoglobulin: variant M107L in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6RYT
Type: protein
Length: 290 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Beta-lactoglobulin
UniProt: P02754
Ligands: PO4
Pockets: 4 · best druggability 0.55

Structure

x-ray diffraction · 2 distinct chains · 17% helix, 43% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Beta-lactoglobulin	protein	145	17% helix, 41% strand	P02754
B	Beta-lactoglobulin	protein	145	16% helix, 44% strand	P02754

Ligands and binding sites

PO4 · Phosphate ion · ion · chains B
GOL · Glycerol · additive · 2 copies · chains A, B

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

Pockets

4 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	284	0.55	0.76	22	empty
2	86	0.49	0.81	16	empty
3	75	0.39	0.78	21	empty
4	72	0.34	0.75	15	PO4

Interfaces

1 interface between chains.

A–B · 544 Å² buried · 9 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 3 disulfide (disulfide).

Compared structures

6RYT · Engineered beta-lactoglobulin: variant M107L · 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 P02754
Elsewhere: RCSB PDB 6RYT · PDBe 6RYT · UniProt P02754

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