MolNFT v1 · #166554 · protein
Allosteric coupling between alpha-rings of the 20S proteasome, 20S singly capped with a PA26/V230F
6UTG: “Allosteric coupling between alpha-rings of the 20S proteasome, 20S singly capped with a PA26/V230F”. Electron microscopy. MolNFT v1 #166554 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6UTG
- Type
- protein
- Length
- 7,525 residues
- Chains
- 35
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P28061, P25156, Q9U8G2
Structure
electron microscopy · 4 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| 1, 2, H, I, J, K, L, M, N, V, W, X, Y, Z | — | protein | 203 | — | P28061 |
| A, B, C, D, E, F, G | — | protein | 227 | — | P25156 |
| O, P, Q, R, S, T, U | — | protein | 218 | — | Q9U8G2 |
| a, b, c, d, e, f, g | — | protein | 224 | — | P25156 |
Compared structures
- 6UTG · Allosteric coupling between alpha-rings of the 20S proteasome, 20S singly capped with a… · the same entry in another collection · chain I against I, 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 P28061
- Every structure of UniProt P25156
- Every structure of UniProt Q9U8G2
- Elsewhere: RCSB PDB 6UTG · PDBe 6UTG · UniProt P28061 · UniProt P25156 · UniProt Q9U8G2
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