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2.9 ångströms resolution structure of the N-terminal domain of a variant surface glycoprotein from trypanosoma brucei

Analyse 2.9 ångströms resolution structure of the N-terminal domain of a variant… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1VSG
Type
protein
Length
724 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Variant surface glycoprotein mitat 1.2
UniProt
P26332
Ligands
NAG, BMA, MAN
Pockets
8 · best druggability 0.82

Structure

x-ray diffraction · 1 distinct chain · 52% helix, 10% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BVariant surface glycoprotein mitat 1.2protein36252% helix, 10% strandP26332

Ligands and binding sites

  • NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 4 copies · chains A, B
  • BMA · beta-D-mannopyranose · sugar · chains A
  • MAN · alpha-D-mannopyranose · sugar · chains B

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11560.820.9828empty
22160.510.7634empty
32250.500.7535empty
41470.430.7534empty
51340.430.7625empty

Interfaces

1 interface between chains.

  • A–B · 4430 Ų buried · 76 hydrogen bonds · protein-protein

Modifications

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

Compared structures

  • 1VSG · 2.9 ångströms resolution structure of the N-terminal domain of a variant surface… · the same entry in another collection · chain A against A, TM-score 1.00
  • P26332 · AlphaFold monomer V2.0 prediction for variant surface glycoprotein mitat 1.2 (P26332) · a predicted model of the same protein · chain A against A, TM-score 1.00

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