Research workbench

Von willebrand factor (vwf) A1 domain with bt-100 aptamer RNA

Analyse Von willebrand factor (vwf) A1 domain with bt-100 aptamer RNA in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7F49
Type: protein + RNA
Length: 228 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Von willebrand factor; Bt-100
UniProt: P04275
Pockets: 2 · best druggability 0.66

Structure

x-ray diffraction · 2 distinct chains · 37% helix, 22% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Von willebrand factor	protein	198	37% helix, 22% strand	P04275
B	Bt-100	rna	30	—	—

Ligands and binding sites

GOL · Glycerol · additive · 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	484	0.66	0.79	32	empty
2	71	0.37	0.78	19	empty

Interfaces

1 interface between chains.

A–B · 1114 Å² buried · 26 hydrogen bonds · protein-nucleic

Modifications

Observed in the structure: 29 modified, 1 disulfide (nucleotide modification, disulfide).

Compared structures

7F49 · von Willebrand factor (VWF) A1 domain with BT-100 aptamer RNA · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt P04275
Elsewhere: RCSB PDB 7F49 · PDBe 7F49 · UniProt P04275

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