Research workbench
Crystal structure of human ALPHA/EPSILON-cop of the copi vesicular coat bound to alpha-cop STM2
Analyse Crystal structure of human ALPHA/EPSILON-cop of the copi vesicular coat bound… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6TZT
- Type
- protein
- Length
- 1,230 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Coatomer subunit epsilon; Coatomer subunit alpha
- UniProt
- O14579, P53621
- Pockets
- 10 · best druggability 0.78
Structure
x-ray diffraction · 4 distinct chains · 63% helix, 4% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Coatomer subunit epsilon | protein | 292 | 74% helix, 0% strand | O14579 |
| B | Coatomer subunit alpha | protein | 330 | 52% helix, 7% strand | P53621 |
| C | Coatomer subunit epsilon | protein | 290 | 74% helix, 0% strand | O14579 |
| D | Coatomer subunit alpha | protein | 318 | 54% helix, 8% strand | P53621 |
Pockets
10 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 746 | 0.78 | 0.82 | 87 | empty |
| 2 | 848 | 0.78 | 0.81 | 94 | empty |
| 3 | 246 | 0.62 | 0.81 | 25 | empty |
| 4 | 201 | 0.59 | 0.81 | 29 | empty |
| 5 | 215 | 0.53 | 0.77 | 27 | empty |
Interfaces
5 interfaces between chains.
- A–B · 2802 Ų buried · 27 hydrogen bonds · protein-protein
- C–D · 2779 Ų buried · 27 hydrogen bonds · protein-protein
- B–C · 595 Ų buried · 8 hydrogen bonds · protein-protein
- A–D · 567 Ų buried · 10 hydrogen bonds · protein-protein
- B–D · 72 Ų buried · 1 hydrogen bond · protein-protein
Compared structures
- 6TZT · Crystal structure of human alpha/epsilon-COP of the COPI vesicular coat bound to… · the same entry in another collection · chain D against D, TM-score 1.00
- O14579 · AlphaFold monomer V2.0 prediction for coatomer subunit epsilon (O14579) · a predicted model of the same protein · chain C against A, TM-score 0.98
- P53621 · AlphaFold monomer V2.0 prediction for coatomer subunit alpha (P53621) · a predicted model of the same protein · chain D 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 O14579
- Every structure of UniProt P53621
- Elsewhere: RCSB PDB 6TZT · PDBe 6TZT · UniProt O14579 · UniProt P53621
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