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Crystal structure of the beta subunit of luteinizing hormone

Analyse Crystal structure of the beta subunit of luteinizing hormone in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6P57
Type
protein
Length
224 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Lutropin subunit beta
UniProt
P04651
Ligands
NAG, BMA, FUL, MAN
Pockets
2 · best druggability 0.78

Structure

x-ray diffraction · 2 distinct chains · 0% helix, 35% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ALutropin subunit betaprotein1060% helix, 40% strandP04651
BLutropin subunit betaprotein1180% helix, 31% strandP04651

Ligands and binding sites

  • NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 5 copies · chains A, B
  • BMA · beta-D-mannopyranose · sugar · 2 copies
  • FUL · beta-L-fucopyranose · sugar · 2 copies · chains A, B
  • MAN · alpha-D-mannopyranose · sugar · 2 copies
  • BOG · octyl beta-D-glucopyranoside · additive · 2 copies · chains 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, 2 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
18290.780.8182empty
24190.570.7441empty

Interfaces

1 interface between chains.

  • A–B · 911 Ų buried · 14 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 12 disulfide, 2 glycan (disulfide, N-glycosylation).

Compared structures

  • 6P57 · Crystal Structure of the Beta Subunit of Luteinizing Hormone · the same entry in another collection · chain A against A, TM-score 1.00
  • P04651 · AlphaFold monomer V2.0 prediction for lutropin subunit beta (P04651) · a predicted model of the same protein · chain A against A, TM-score 0.73

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