Research workbench
Crystal structure of the CCM2 C-terminal harmonin homology domain (hhd)
Analyse Crystal structure of the CCM2 C-terminal harmonin homology domain (hhd) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4FQN
- Type
- protein
- Length
- 350 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Malcavernin
- UniProt
- Q9BSQ5
- Pockets
- 2 · best druggability 0.49
Structure
x-ray diffraction · 4 distinct chains · 77% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Malcavernin | protein | 95 | 75% helix, 0% strand | Q9BSQ5 |
| B | Malcavernin | protein | 93 | 78% helix, 0% strand | Q9BSQ5 |
| C | Malcavernin | protein | 85 | 74% helix, 0% strand | Q9BSQ5 |
| D | Malcavernin | protein | 77 | 81% helix, 0% strand | Q9BSQ5 |
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 173 | 0.49 | 0.77 | 23 | empty |
| 2 | 145 | 0.44 | 0.76 | 26 | empty |
Interfaces
5 interfaces between chains.
- A–B · 1016 Ų buried · 15 hydrogen bonds · protein-protein
- A–C · 505 Ų buried · 5 hydrogen bonds · protein-protein
- B–D · 460 Ų buried · 5 hydrogen bonds · protein-protein
- A–D · 459 Ų buried · 13 hydrogen bonds · protein-protein
- B–C · 340 Ų buried · 4 hydrogen bonds · protein-protein
Compared structures
- 4FQN · Crystal structure of the CCM2 C-terminal Harmonin Homology Domain (HHD) · the same entry in another collection · chain D against D, TM-score 1.00
- Q9BSQ5 · AlphaFold monomer V2.0 prediction for cerebral cavernous malformations 2 protein (Q9BSQ5) · a predicted model of the same protein · chain D against A, TM-score 0.92
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 Q9BSQ5
- Elsewhere: RCSB PDB 4FQN · PDBe 4FQN · UniProt Q9BSQ5
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