Research workbench
Re-refinement of integrin ALPHAIIBBETA3 headpiece
Analyse Re-refinement of integrin ALPHAIIBBETA3 headpiece in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2VDK
- Type
- protein
- Length
- 1,340 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Integrin alpha-iib; Integrin beta-3; Monoclonal antibody 10E5 heavy chain; Monoclonal…
- UniProt
- P08514, P05106
- Ligands
- MAN, NAG, CA, MG
- Pockets
- 14 · best druggability 0.78
Structure
x-ray diffraction · 4 distinct chains · 12% helix, 40% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Integrin alpha-iib | protein | 452 | 6% helix, 42% strand | P08514 |
| B | Integrin beta-3 | protein | 455 | 24% helix, 28% strand | P05106 |
| H | Monoclonal antibody 10E5 heavy chain | protein | 219 | 5% helix, 51% strand | — |
| L | Monoclonal antibody 10E5 light chain | protein | 214 | 6% helix, 51% strand | — |
Ligands and binding sites
- MAN · alpha-D-mannopyranose · sugar · 8 copies · chains A
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 7 copies · chains A, B
- CA · Calcium ion · metal · 6 copies · chains A, B
- MG · Magnesium ion · metal · chains B
- GOL · Glycerol · additive · 2 copies · chains A, B
- CAC · Cacodylate ion · additive · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
14 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 681 | 0.78 | 0.83 | 53 | empty |
| 2 | 689 | 0.75 | 0.81 | 63 | empty |
| 3 | 185 | 0.53 | 0.78 | 30 | GOL |
| 4 | 262 | 0.49 | 0.74 | 44 | empty |
| 5 | 53 | 0.47 | 0.85 | 13 | empty |
Interfaces
4 interfaces between chains.
- H–L · 1996 Ų buried · 16 hydrogen bonds · protein-protein
- A–B · 1743 Ų buried · 22 hydrogen bonds · protein-protein
- A–H · 632 Ų buried · 9 hydrogen bonds · protein-protein
- A–L · 401 Ų buried · 7 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 18 disulfide, 5 glycan (disulfide, N-glycosylation).
Compared structures
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 P08514
- Every structure of UniProt P05106
- Elsewhere: RCSB PDB 2VDK · PDBe 2VDK · UniProt P08514 · UniProt P05106
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.