Research workbench
Thermoplasma acidophilum 20S proteasome using 200KEV with image shift
Analyse Thermoplasma acidophilum 20S proteasome using 200KEV with image shift in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5VY4
- Type
- protein
- Length
- 5,936 residues
- Chains
- 28
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P25156, P28061
Structure
electron microscopy · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C, E, G, I, K, M, O, Q, S, U, W, Y, 0 | — | protein | 221 | — | P25156 |
| B, D, F, H, J, L, N, P, R, T, V, X, Z, 1 | — | protein | 203 | — | P28061 |
Compared structures
- 5VY4 · Thermoplasma acidophilum 20S Proteasome using 200keV with image shift · the same entry in another collection · chain K against K, TM-score 1.00
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 P25156
- Every structure of UniProt P28061
- Elsewhere: RCSB PDB 5VY4 · PDBe 5VY4 · UniProt P25156 · UniProt P28061
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