Research workbench
Crystal structure of actin capping protein in complex with carmil fragment
Analyse Crystal structure of actin capping protein in complex with carmil fragment in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3AAE
- Type
- protein
- Length
- 2,758 residues
- Chains
- 15
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- F-actin-capping protein subunit alpha-1; F-actin-capping protein subunit beta isoforms 1…
- UniProt
- P13127, P14315, Q6EDY6
- Pockets
- 20 · best druggability 0.80
Structure
x-ray diffraction · 8 distinct chains · 36% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C, E, G, I | F-actin-capping protein subunit alpha-1 | protein | 270 | 38% helix, 34% strand | P13127 |
| B, D | F-actin-capping protein subunit beta isoforms 1 and 2 | protein | 264 | 41% helix, 31% strand | P14315 |
| F | F-actin-capping protein subunit beta isoforms 1 and 2 | protein | 250 | 38% helix, 33% strand | P14315 |
| H, J | F-actin-capping protein subunit beta isoforms 1 and 2 | protein | 249 | 38% helix, 33% strand | P14315 |
| X | 32MER peptide from leucine-rich repeat-containing protein 16A | protein | 29 | 0% helix, 0% strand | Q6EDY6 |
| Y, Z | 32MER peptide from leucine-rich repeat-containing protein 16A | protein | 28 | 0% helix, 0% strand | Q6EDY6 |
| W | 32MER peptide from leucine-rich repeat-containing protein 16A | protein | 26 | 15% helix, 0% strand | Q6EDY6 |
| V | 32MER peptide from leucine-rich repeat-containing protein 16A | protein | 21 | 19% helix, 0% strand | Q6EDY6 |
Pockets
20 pockets found on a 1 Å grid, 11 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 120 | 0.80 | 0.98 | 21 | empty |
| 2 | 112 | 0.80 | 0.99 | 20 | empty |
| 3 | 124 | 0.80 | 0.98 | 22 | empty |
| 4 | 112 | 0.79 | 0.98 | 18 | empty |
| 5 | 104 | 0.78 | 0.98 | 18 | empty |
Interfaces
29 interfaces between chains.
- A–B · 4060 Ų buried · 62 hydrogen bonds · protein-protein
- I–J · 3990 Ų buried · 58 hydrogen bonds · protein-protein
- G–H · 3986 Ų buried · 60 hydrogen bonds · protein-protein
- E–F · 3978 Ų buried · 60 hydrogen bonds · protein-protein
- C–D · 3956 Ų buried · 59 hydrogen bonds · protein-protein
Compared structures
- 3AAE · Crystal structure of Actin capping protein in complex with CARMIL fragment · the same entry in another collection · chain H against H, 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 P13127
- Every structure of UniProt P14315
- Every structure of UniProt Q6EDY6
- Elsewhere: RCSB PDB 3AAE · PDBe 3AAE · UniProt P13127 · UniProt P14315 · UniProt Q6EDY6
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