MolNFT v1 · #186348 · protein
AlphaFold monomer V2.0 prediction for eukaryotic translation initiation factor 5 (P55010)
P55010: “AlphaFold monomer V2.0 prediction for eukaryotic translation initiation factor 5 (P55010)”. MolNFT v1 #186348 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- Accession
- P55010
- Type
- protein
- Length
- 431 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x84Aa208e2B591Ce293F973D0D4D2B8b20986E9ca
- UniProt
- P55010
Structure
1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 431 | — | P55010 |
Compared structures
- 2IU1 · Crystal structure of eIF5 C-terminal domain · an experimental structure of the same protein · chain A against A, TM-score 0.39
- 2IU1 · Crystal structure of EIF5 C-terminal domain · an experimental structure of the same protein · chain A against A, TM-score 0.39
- 2E9H · Solution structure of the eIF-5_eIF-2B domain from human Eukaryotic translation… · an experimental structure of the same protein · chain A against A, TM-score 0.33
- 2E9H · Solution structure of the eif-5_EIF-2B domain from human eukaryotic translation… · an experimental structure of the same protein · chain A against A, TM-score 0.33
- 2G2K · NMR structure of an N-terminal fragment of the eukaryotic initiation factor 5 (eIF5) · an experimental structure of the same protein · chain A against A, TM-score 0.21
- 2G2K · NMR structure of an N-terminal fragment of the eukaryotic initiation factor 5 (EIF5) · an experimental structure of the same protein · chain A against A, TM-score 0.21
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 P55010
- Elsewhere: UniProt P55010 · AlphaFold DB P55010
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