MolNFT v1 · #86601 · protein
Cryo-electron microscopy reconstruction of the helical part of influenza a virus ribonucleoprotein isolated from virions.
4BBL: “Cryo-electron microscopy reconstruction of the helical part of influenza a virus ribonucleoprotein isolated…”. Electron microscopy. MolNFT v1 #86601 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 4BBL
- Type
- protein
- Length
- 9,906 residues
- Chains
- 24
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P15682
Structure
electron microscopy · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R, S, T, U, V, X | — | protein | 414 | — | P15682 |
| B, W | — | protein | 399 | — | P15682 |
Compared structures
- 4BBL · Cryo-electron microscopy reconstruction of the helical part of influenza A virus… · the same entry in another collection · chain D against D, 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 P15682
- Elsewhere: RCSB PDB 4BBL · PDBe 4BBL · UniProt P15682
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