MolNFT v1 · #113880 · protein
AlphaFold monomer V2.0 prediction for elongation factor tu, mitochondrial (P49410)
P49410: “AlphaFold monomer V2.0 prediction for elongation factor tu, mitochondrial (P49410)”. MolNFT v1 #113880 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- Accession
- P49410
- Type
- protein
- Length
- 452 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xbDA05C32aD6eE153C8C5A78dfa48d7Ba25694fea
- UniProt
- P49410
Structure
1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 452 | — | P49410 |
Compared structures
- 1D2E · Crystal structure of mitochondrial ef-tu in complex with GDP · an experimental structure of the same protein · chain A against B, TM-score 0.51
- 1D2E · Crystal structure of mitochondrial ef-tu in complex with GDP · an experimental structure of the same protein · chain A against B, TM-score 0.51
- 1XB2 · Crystal Structure of Bos taurus mitochondrial Elongation Factor Tu/Ts Complex · an experimental structure of the same protein · chain A against A, TM-score 0.44
- 1XB2 · Crystal structure of bos taurus mitochondrial elongation factor TU/TS complex · an experimental structure of the same protein · chain A against A, TM-score 0.44
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 P49410
- Elsewhere: UniProt P49410 · AlphaFold DB P49410
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