Research workbench
Crystal structure of a complex between integrin BETA4 and plectin
Analyse Crystal structure of a complex between integrin BETA4 and plectin in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3F7P
- Type
- protein
- Length
- 1,069 residues
- Chains
- 5
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Plectin-1; Integrin beta-4
- UniProt
- Q15149, P16144
- Ligands
- CA
- Pockets
- 9 · best druggability 0.75
Structure
x-ray diffraction · 5 distinct chains · 25% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Plectin-1 | protein | 231 | 59% helix, 1% strand | Q15149 |
| B | Plectin-1 | protein | 230 | 59% helix, 1% strand | Q15149 |
| C | Integrin beta-4 | protein | 200 | 0% helix, 48% strand | P16144 |
| D | Integrin beta-4 | protein | 196 | 0% helix, 48% strand | P16144 |
| E | Integrin beta-4 | protein | 212 | 0% helix, 48% strand | P16144 |
Ligands and binding sites
- CA · Calcium ion · metal · chains D
- EDO · 1,2-ethanediol · additive · 2 copies · chains A, B
- PEG · Di(hydroxyethyl)ether · additive · chains B, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
9 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 970 | 0.75 | 0.78 | 110 | EDO |
| 2 | 790 | 0.73 | 0.78 | 89 | empty |
| 3 | 82 | 0.52 | 0.85 | 23 | empty |
| 4 | 104 | 0.38 | 0.75 | 17 | empty |
| 5 | 56 | 0.38 | 0.80 | 16 | empty |
Interfaces
7 interfaces between chains.
- C–D · 1470 Ų buried · 37 hydrogen bonds · protein-protein
- A–C · 1205 Ų buried · 26 hydrogen bonds · protein-protein
- B–D · 1130 Ų buried · 18 hydrogen bonds · protein-protein
- A–E · 729 Ų buried · 5 hydrogen bonds · protein-protein
- C–E · 461 Ų buried · 8 hydrogen bonds · protein-protein
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 Q15149
- Every structure of UniProt P16144
- Elsewhere: RCSB PDB 3F7P · PDBe 3F7P · UniProt Q15149 · UniProt P16144
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