Research workbench
Crystal structure of yeast ALPHA/EPSILON-cop subcomplex of the copi vesicular coat
Analyse Crystal structure of yeast ALPHA/EPSILON-cop subcomplex of the copi vesicular… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3MKR
- Type
- protein
- Length
- 611 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Coatomer subunit epsilon; Coatomer subunit alpha
- UniProt
- Q28104, Q27954
- Pockets
- 5 · best druggability 0.78
Structure
x-ray diffraction · 2 distinct chains · 63% helix, 3% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Coatomer subunit epsilon | protein | 291 | 76% helix, 0% strand | Q28104 |
| B | Coatomer subunit alpha | protein | 320 | 51% helix, 7% strand | Q27954 |
Pockets
5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 882 | 0.78 | 0.81 | 91 | empty |
| 2 | 299 | 0.57 | 0.77 | 56 | empty |
| 3 | 202 | 0.50 | 0.76 | 27 | empty |
| 4 | 144 | 0.49 | 0.78 | 19 | empty |
| 5 | 91 | 0.46 | 0.81 | 16 | empty |
Interfaces
1 interface between chains.
- A–B · 2751 Ų buried · 21 hydrogen bonds · protein-protein
Compared structures
- 3MKR · Crystal structure of yeast alpha/epsilon-COP subcomplex of the COPI vesicular coat · the same entry in another collection · chain A against A, TM-score 1.00
- Q28104 · AlphaFold monomer V2.0 prediction for coatomer subunit epsilon (Q28104) · a predicted model of the same protein · chain A against A, TM-score 0.99
- Q27954 · AlphaFold monomer V2.0 prediction for coatomer subunit alpha (Q27954) · a predicted model of the same protein · chain B against A, TM-score 0.96
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 Q28104
- Every structure of UniProt Q27954
- Elsewhere: RCSB PDB 3MKR · PDBe 3MKR · UniProt Q28104 · UniProt Q27954
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