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Crystal structure of glycoprotein VI in complex with collagen-peptide (GPO)5

Analyse Crystal structure of glycoprotein VI in complex with collagen-peptide (GPO)5 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5OU8
Type
protein
Length
388 residues
Chains
5
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Platelet glycoprotein VI; (GPO)5
UniProt
Q9HCN6
Ligands
NAG, CL

Structure

x-ray diffraction · 3 distinct chains · 2% helix, 48% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
APlatelet glycoprotein VIprotein1742% helix, 49% strandQ9HCN6
BPlatelet glycoprotein VIprotein1692% helix, 52% strandQ9HCN6
C, D, E(GPO)5protein150% helix, 0% strand—

Ligands and binding sites

  • NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 2 copies · chains A, B
  • CL · Chloride ion · ion · 2 copies · chains A, B
  • PG4 · Tetraethylene glycol · additive · 2 copies · chains A, B

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

Interfaces

8 interfaces between chains.

  • C–D · 478 Ų buried · 5 hydrogen bonds · protein-protein
  • D–E · 475 Ų buried · 4 hydrogen bonds · protein-protein
  • C–E · 420 Ų buried · 7 hydrogen bonds · protein-protein
  • A–E · 295 Ų buried · 5 hydrogen bonds · protein-protein
  • B–D · 288 Ų buried · 4 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 15 modified, 4 disulfide, 2 glycan (hydroxylation, disulfide, N-glycosylation).

Compared structures

  • 5OU8 · Crystal structure of Glycoprotein VI in complex with collagen-peptide (GPO)5 · the same entry in another collection · chain B against B, TM-score 1.00
  • Q9HCN6 · AlphaFold monomer V2.0 prediction for platelet glycoprotein VI (Q9HCN6) · a predicted model of the same protein · chain A against A, TM-score 0.92

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