MolNFT v1 · #90384 · protein
Crystal structure of human vinculin head domain (residues 1-252) in complex with alpha-catenin (residues 277-382)
4EHP: “Crystal structure of human vinculin head domain (residues 1-252) in complex with alpha-catenin (residues…”. X-ray diffraction, 1 pocket (best druggability 0.70). MolNFT v1 #90384 on GenesisL1: 3D structure, binding sites and pockets…
- PDB
- 4EHP
- Type
- protein
- Length
- 341 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Vinculin; Catenin alpha-1
- UniProt
- P18206, P35221
- Pockets
- 1 · best druggability 0.70
Structure
x-ray diffraction · 2 distinct chains · 79% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Vinculin | protein | 248 | 81% helix, 1% strand | P18206 |
| B | Catenin alpha-1 | protein | 93 | 73% helix, 0% strand | P35221 |
Ligands and binding sites
- ACT · Acetate ion · additive · 9 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 469 | 0.70 | 0.81 | 39 | ACT |
Interfaces
1 interface between chains.
- A–B · 2306 Ų buried · 13 hydrogen bonds · protein-protein
Compared structures
- 4EHP · Crystal Structure of human vinculin head domain (residues 1-252) in complex with… · 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 0.90
- P35221 · AlphaFold monomer V2.0 prediction for catenin alpha-1 (P35221) · a predicted model of the same protein · chain B against A, TM-score 0.46
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
- Every structure of UniProt P35221
- Elsewhere: RCSB PDB 4EHP · PDBe 4EHP · UniProt P18206 · UniProt P35221
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