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
- 3MV3
- Type
- protein
- Length
- 1,788 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 · 2 distinct chains · 59% helix, 5% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C, E | Coatomer subunit alpha | protein | 303 | 50% helix, 9% strand | P53622 |
| B, D, F | Coatomer subunit epsilon | protein | 293 | 68% helix, 0% strand | P40509 |
Pockets
20 pockets found on a 1 Å grid, 12 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 986 | 0.78 | 0.80 | 102 | empty |
| 2 | 963 | 0.75 | 0.78 | 59 | empty |
| 3 | 931 | 0.75 | 0.78 | 62 | empty |
| 4 | 484 | 0.68 | 0.79 | 64 | empty |
| 5 | 467 | 0.66 | 0.78 | 70 | empty |
Interfaces
8 interfaces between chains.
- C–D · 2396 Ų buried · 27 hydrogen bonds · protein-protein
- A–B · 2395 Ų buried · 28 hydrogen bonds · protein-protein
- E–F · 2332 Ų buried · 26 hydrogen bonds · protein-protein
- A–D · 798 Ų buried · 8 hydrogen bonds · protein-protein
- C–F · 688 Ų buried · 7 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 30 modified (engineered).
Compared structures
- 3MV3 · 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 3MV3 · PDBe 3MV3 · UniProt P53622 · UniProt P40509
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