GL1X · GenesisL1 explorer

Research workbench

Crystal structure of alpha-lactalbumin

Analyse Crystal structure of alpha-lactalbumin in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3B0O
Type
protein
Length
240 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Alpha-lactalbumin
UniProt
P00709
Ligands
CA
Pockets
2 · best druggability 0.50

Structure

x-ray diffraction · 1 distinct chain · 44% helix, 12% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BAlpha-lactalbuminprotein12044% helix, 12% strandP00709

Ligands and binding sites

  • CA · Calcium 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, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11980.500.7632empty
2860.340.7415empty

Interfaces

1 interface between chains.

  • A–B · 425 Ų buried · 2 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 8 disulfide (disulfide).

Compared structures

  • 3B0O · Crystal structure of alpha-lactalbumin · the same entry in another collection · chain A against A, TM-score 1.00
  • P00709 · AlphaFold monomer V2.0 prediction for alpha-lactalbumin (P00709) · a predicted model of the same protein · chain A against A, TM-score 0.90

Analyse

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.