Research workbench
Cryogenic electron microscopy model of full-length human metavinculin H1'-parallel conformation 1
Analyse Cryogenic electron microscopy model of full-length human metavinculin… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7KTU
- Type
- protein
- Length
- 995 residues
- Chains
- 1
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Metavinculin
- UniProt
- P18206
- Pockets
- 15 · best druggability 0.83
Structure
electron microscopy · 1 distinct chain · 77% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Metavinculin | protein | 995 | 77% helix, 0% strand | P18206 |
Pockets
15 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1181 | 0.83 | 0.84 | 124 | empty |
| 2 | 539 | 0.79 | 0.85 | 51 | empty |
| 3 | 132 | 0.78 | 0.95 | 20 | empty |
| 4 | 425 | 0.69 | 0.81 | 48 | empty |
| 5 | 104 | 0.64 | 0.88 | 23 | empty |
Compared structures
- 7KTU · Cryogenic electron microscopy model of full-length human metavinculin H1'-parallel… · the same entry in another collection · chain A against A, TM-score 1.00
- P18206 · AlphaFold monomer V2.0 prediction for vinculin (P18206) · a predicted model of the same protein · chain A against A, TM-score 0.94
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 P18206
- Elsewhere: RCSB PDB 7KTU · PDBe 7KTU · UniProt P18206
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