Research workbench
Cryo-EM structure of vwf D'D3 dimer (2M mutant) complexed with D1D2 at 3.29 angstron resolution (2 units)
Analyse Cryo-EM structure of vwf D'D3 dimer (2M mutant) complexed with D1D2 at 3.29… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7WN3
- Type
- protein
- Length
- 4,756 residues
- Chains
- 8
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P04275
- Ligands
- NAG, CA
Structure
electron microscopy · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, E, G | — | protein | 711 | — | P04275 |
| F, H, C, D | — | protein | 478 | — | P04275 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 20 copies · chains A, F, B, H, E, G, C, D
- CA · Calcium ion · metal · 16 copies · chains A, F, B, H, E, G, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7WN3 · Cryo-EM structure of VWF D'D3 dimer (2M mutant) complexed with D1D2 at 3.29 angstron… · 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 7WN3 · PDBe 7WN3 · UniProt P04275
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