Research workbench
Fitted structure of adpr-EEF2 in the 80S:ADPR-EEF2:GDPNP cryo-EM reconstruction
Analyse Fitted structure of adpr-EEF2 in the 80S:ADPR-EEF2:GDPNP cryo-EM reconstruction in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2P8X
- Type
- protein
- Length
- 849 residues
- Chains
- 2
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P32324, P60339
Structure
electron microscopy · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| T | — | protein | 814 | — | P32324 |
| S | — | protein | 35 | — | P60339 |
Compared structures
- 2P8X · Fitted structure of ADPR-eEF2 in the 80S:ADPR-eEF2:GDPNP cryo-EM reconstruction · the same entry in another collection · chain T against T, TM-score 1.00
- P60339 · AlphaFold monomer V2.0 prediction for elongation factor tu-B (P60339) · a predicted model of the same protein · chain S against A, TM-score 0.91
- P32324 · AlphaFold monomer V2.0 prediction for elongation factor 2 (P32324) · a predicted model of the same protein · chain T against A, TM-score 0.70
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 P32324
- Every structure of UniProt P60339
- Elsewhere: RCSB PDB 2P8X · PDBe 2P8X · UniProt P32324 · UniProt P60339
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