Research workbench
Crystal structure of the archaeal EF1A-EF1B complex
Analyse Crystal structure of the archaeal EF1A-EF1B complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7CSL
- Type
- protein
- Length
- 1,018 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- O59153, P58748
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | — | protein | 421 | — | O59153 |
| C, D | — | protein | 88 | — | P58748 |
Compared structures
- P58748 · AlphaFold monomer V2.0 prediction for elongation factor 1-beta (P58748) · a predicted model of the same protein · chain D against A, TM-score 0.98
- O59153 · AlphaFold monomer V2.0 prediction for elongation factor 1-alpha (O59153) · a predicted model of the same protein · chain B against A, TM-score 0.73
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 O59153
- Every structure of UniProt P58748
- Elsewhere: RCSB PDB 7CSL · PDBe 7CSL · UniProt O59153 · UniProt P58748
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