MolNFT v1 · #70771 · protein
Model of alpha-actinin CH1 bound to F-actin
3LUE · Actin, cytoplasmic 1: “Model of alpha-actinin CH1 bound to F-actin”. Electron microscopy, 20 pockets (best druggability 0.76). MolNFT v1 #70771 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 3LUE
- Type
- protein
- Length
- 4,830 residues
- Chains
- 20
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Actin, cytoplasmic 1; Alpha-actinin-3
- UniProt
- P60709, Q08043
- Pockets
- 20 · best druggability 0.76
Structure
electron microscopy · 2 distinct chains · 46% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G, H, I, J | Actin, cytoplasmic 1 | protein | 374 | 41% helix, 20% strand | P60709 |
| K, M, L, O, N, Q, P, S, R, T | Alpha-actinin-3 | protein | 109 | 62% helix, 0% strand | Q08043 |
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 465 | 0.76 | 0.85 | 65 | empty |
| 2 | 545 | 0.76 | 0.83 | 68 | empty |
| 3 | 575 | 0.76 | 0.83 | 67 | empty |
| 4 | 455 | 0.76 | 0.84 | 66 | empty |
| 5 | 660 | 0.75 | 0.81 | 73 | empty |
Interfaces
35 interfaces between chains.
- B–D · 1408 Ų buried · 78 hydrogen bonds · protein-protein
- F–H · 1408 Ų buried · 78 hydrogen bonds · protein-protein
- A–C · 1407 Ų buried · 79 hydrogen bonds · protein-protein
- G–I · 1403 Ų buried · 78 hydrogen bonds · protein-protein
- E–G · 1403 Ų buried · 78 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 10 isopeptide (isopeptide).
Compared structures
- 3LUE · Model of alpha-actinin CH1 bound to F-actin · the same entry in another collection · chain G against G, TM-score 1.00
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 P60709
- Every structure of UniProt Q08043
- Elsewhere: RCSB PDB 3LUE · PDBe 3LUE · UniProt P60709 · UniProt Q08043
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