MolNFT v1 · #115678 · protein
Dimerization of ELP1 is essential for elongator complex assembly
5CQR: “Dimerization of ELP1 is essential for elongator complex assembly”. X-ray diffraction. MolNFT v1 #115678 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 5CQR
- Type
- protein
- Length
- 455 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- O95163
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 455 | — | O95163 |
Compared structures
- O95163 · AlphaFold monomer V2.0 prediction for elongator complex protein 1 (O95163) · a predicted model of the same protein · chain A against A, TM-score 0.81
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 O95163
- Elsewhere: RCSB PDB 5CQR · PDBe 5CQR · UniProt O95163
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