GL1X · GenesisL1 explorer

Research workbench

Rfviiifc-vwf-xten (BIVV001)

Analyse Rfviiifc-vwf-xten (BIVV001) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7KWO
Type
protein
Length
1,678 residues
Chains
2
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Coagulation factor fviii-Fc-xten; Von willebrand factor-xten-Fc
Ligands
NAG, BMA, CA, ZN, CU
Pockets
20 · best druggability 0.86

Structure

electron microscopy · 2 distinct chains · 10% helix, 41% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ACoagulation factor fviii-Fc-xtenprotein12008% helix, 44% strand—
VVon willebrand factor-xten-Fcprotein47814% helix, 32% strand—

Ligands and binding sites

  • NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 5 copies · chains A, V
  • BMA · beta-D-mannopyranose · sugar
  • CA · Calcium ion · metal · 2 copies · chains A, V
  • ZN · Zinc ion · metal · chains A
  • CU · Copper (II) ion · metal · chains A

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

Pockets

20 pockets found on a 1 Å grid, 13 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
18250.860.8987empty
29050.790.8293empty
310360.740.77130empty
4600.680.9624empty
56010.680.7751empty

Interfaces

1 interface between chains.

  • A–V · 2568 Ų buried · 21 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 32 disulfide, 4 glycan, 1 modified (disulfide, N-glycosylation, sulfation).

Compared structures

  • 7KWO · rFVIIIFc-VWF-XTEN (BIVV001) · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

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