MolNFT v1 · #166555 · protein
Allosteric coupling between alpha-rings of 20S proteasome, 20S proteasome singly capped with a PA26/E102A_PANC, together with lfp incubation
6UTH: “Allosteric coupling between alpha-rings of 20S proteasome, 20S proteasome singly capped with a…”. Electron microscopy. MolNFT v1 #166555 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6UTH
- Type
- protein
- Length
- 7,553 residues
- Chains
- 35
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P25156, P28061, Q38BM8
Structure
electron microscopy · 4 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G | — | protein | 227 | — | P25156 |
| Z, M, 1, N, 2, H, V, I, W, J, X, K, Y, L | — | protein | 203 | — | P28061 |
| O, P, Q, R, S, T, U | — | protein | 227 | — | P25156 |
| a, b, c, d, e, f, g | — | protein | 219 | — | Q38BM8 |
Compared structures
- 6UTH · Allosteric coupling between alpha-rings of 20S proteasome, 20S proteasome singly capped… · the same entry in another collection · chain 1 against 1, 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
- Every structure of UniProt Q38BM8
- Elsewhere: RCSB PDB 6UTH · PDBe 6UTH · UniProt P25156 · UniProt P28061 · UniProt Q38BM8
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