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Structure of mitat 1.1

Analyse Structure of mitat 1.1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5LY9
Type
protein
Length
732 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Variant surface glycoprotein mitat 1.1
UniProt
P26331
Ligands
NAG, MAN, BMA
Pockets
5 · best druggability 0.64

Structure

x-ray diffraction · 2 distinct chains · 52% helix, 7% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AVariant surface glycoprotein mitat 1.1protein36852% helix, 7% strandP26331
BVariant surface glycoprotein mitat 1.1protein36452% helix, 7% strandP26331

Ligands and binding sites

  • NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 4 copies · chains A, B
  • MAN · alpha-D-mannopyranose · sugar · 4 copies · chains A, B
  • BMA · beta-D-mannopyranose · sugar · 2 copies · chains A, B
  • GOL · Glycerol · additive · 6 copies · chains A, B
  • MES · 2-(N-morpholino)-ethanesulfonic acid · additive · chains B

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

Pockets

5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1990.640.8925empty
22280.520.7740GOL
32030.500.7634GOL
41450.460.7731NAG, GOL
51440.440.7627NAG, GOL

Interfaces

1 interface between chains.

  • A–B · 4307 Ų buried · 66 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 disulfide, 2 glycan (disulfide, N-glycosylation).

Compared structures

  • 5LY9 · Structure of MITat 1.1 · the same entry in another collection · chain A against A, TM-score 1.00
  • P26331 · AlphaFold monomer V2.0 prediction for variant surface glycoprotein mitat 1.1 (P26331) · a predicted model of the same protein · chain A against A, TM-score 1.00

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