MolNFT v1 · #165705 · protein
Crystal structure of yeast ALPHA/EPSILON-cop of the copi vesicular coat
6U3W: “Crystal structure of yeast ALPHA/EPSILON-cop of the copi vesicular coat”. X-ray diffraction. MolNFT v1 #165705 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6U3W
- Type
- protein
- Length
- 594 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P53622, P40509
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 303 | — | P53622 |
| B | — | protein | 291 | — | P40509 |
Ligands and binding sites
- GOL · Glycerol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6U3W · Crystal structure of yeast alpha/epsilon-COP of the COPI vesicular coat · the same entry in another collection · chain A against A, TM-score 1.00
- P53622 · AlphaFold monomer V2.0 prediction for coatomer subunit alpha (P53622) · a predicted model of the same protein · chain A against A, TM-score 0.98
- P40509 · AlphaFold monomer V2.0 prediction for coatomer subunit epsilon (P40509) · a predicted model of the same protein · chain B 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 6U3W · PDBe 6U3W · UniProt P53622 · UniProt P40509
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