Research workbench
Second pair of Fibronectin type III domains of integrin beta4 (T1663R mutant) bound to the bullous pemphigoid antigen BP230 (BPAG1e)
Analyse Second pair of Fibronectin type III domains of integrin beta4 (T1663R mutant)… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6GVK
- Type
- protein
- Length
- 225 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.55
- Source
- Homo sapiens; SYNTHETIC CONSTRUCT
- Molecule
- Integrin beta-4; Dystonin
- UniProt
- P16144, Q03001
- Pockets
- 1 · best druggability 0.44
Structure
x-ray diffraction · resolution 1.55 · 2 distinct chains · 0% helix, 55% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Integrin beta-4 | protein | 201 | 0% helix, 56% strand | P16144 |
| B | Dystonin | protein | 24 | 0% helix, 46% strand | Q03001 |
Ligands and binding sites
- GOL · Glycerol · additive · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 146 | 0.44 | 0.76 | 22 | empty |
Interfaces
1 interface between chains.
- A–B · 1635 Ų buried · 32 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 6GVK · Second pair of fibronectin type III domains of integrin BETA4 (T1663R mutant) bound to… · the same entry in another collection · chain A against A, TM-score 1.00
- P16144 · AlphaFold monomer V2.0 prediction for integrin beta-4 (P16144) · a predicted model of the same protein · chain A against A, TM-score 0.58
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 P16144
- Every structure of UniProt Q03001
- Elsewhere: RCSB PDB 6GVK · PDBe 6GVK · UniProt P16144 · UniProt Q03001
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