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Crystal structure of alpha-COP/E19 complex
Analyse Crystal structure of alpha-COP/E19 complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4J8G
- Type
- protein
- Length
- 620 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Coatomer subunit alpha; Membrane glycoprotein E3 GP19K
- UniProt
- Q96WV5
- Pockets
- 3 · best druggability 0.86
Structure
x-ray diffraction · 4 distinct chains · 3% helix, 55% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Coatomer subunit alpha | protein | 298 | 0% helix, 58% strand | Q96WV5 |
| B | Coatomer subunit alpha | protein | 302 | 1% helix, 57% strand | Q96WV5 |
| C | Membrane glycoprotein E3 GP19K | protein | 11 | 64% helix, 0% strand | — |
| D | Membrane glycoprotein E3 GP19K | protein | 9 | 67% helix, 0% strand | — |
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 970 | 0.86 | 0.87 | 74 | empty |
| 2 | 722 | 0.83 | 0.87 | 55 | empty |
| 3 | 150 | 0.46 | 0.77 | 30 | empty |
Interfaces
4 interfaces between chains.
- A–B · 474 Ų buried · 4 hydrogen bonds · protein-protein
- B–C · 437 Ų buried · 16 hydrogen bonds · protein-protein
- A–D · 411 Ų buried · 14 hydrogen bonds · protein-protein
- B–D · 228 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
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 Q96WV5
- Elsewhere: RCSB PDB 4J8G · PDBe 4J8G · UniProt Q96WV5
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