Research workbench
Crystal structure of a-cop in complex with E-cop
Analyse Crystal structure of a-cop in complex with E-cop in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3MV2
- Type
- protein
- Length
- 1,790 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Coatomer subunit alpha; Coatomer subunit epsilon
- UniProt
- P53622, P40509
- Pockets
- 20 · best druggability 0.78
Structure
x-ray diffraction · 3 distinct chains · 58% helix, 6% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Coatomer subunit alpha | protein | 305 | 53% helix, 9% strand | P53622 |
| B, D, F | Coatomer subunit epsilon | protein | 293 | 70% helix, 0% strand | P40509 |
| C, E | Coatomer subunit alpha | protein | 303 | 53% helix, 9% strand | P53622 |
Pockets
20 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 951 | 0.78 | 0.80 | 106 | empty |
| 2 | 909 | 0.73 | 0.77 | 64 | empty |
| 3 | 779 | 0.70 | 0.77 | 44 | empty |
| 4 | 448 | 0.69 | 0.80 | 67 | empty |
| 5 | 705 | 0.68 | 0.76 | 56 | empty |
Interfaces
8 interfaces between chains.
- A–B · 2426 Ų buried · 26 hydrogen bonds · protein-protein
- C–D · 2364 Ų buried · 28 hydrogen bonds · protein-protein
- E–F · 2332 Ų buried · 21 hydrogen bonds · protein-protein
- A–D · 752 Ų buried · 6 hydrogen bonds · protein-protein
- C–F · 596 Ų buried · 4 hydrogen bonds · protein-protein
Compared structures
- 3MV2 · Crystal Structure of a-COP in Complex with e-COP · the same entry in another collection · chain F against F, TM-score 1.00
- P40509 · AlphaFold monomer V2.0 prediction for coatomer subunit epsilon (P40509) · a predicted model of the same protein · chain D against A, TM-score 0.97
- P53622 · AlphaFold monomer V2.0 prediction for coatomer subunit alpha (P53622) · a predicted model of the same protein · chain A against A, TM-score 0.97
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 P53622
- Every structure of UniProt P40509
- Elsewhere: RCSB PDB 3MV2 · PDBe 3MV2 · UniProt P53622 · UniProt P40509
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