Research workbench
Crystal structure analysis of eukaryotic translation initiation factor 5B and 1A complex
Analyse Crystal structure analysis of eukaryotic translation initiation factor 5B and… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3WBK
- Type
- protein
- Length
- 1,191 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P39730, P38912
Structure
x-ray diffraction · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 590 | — | P39730 |
| B | — | protein | 590 | — | P39730 |
| C | — | protein | 11 | — | P38912 |
Compared structures
- 3WBK · crystal structure analysis of eukaryotic translation initiation factor 5B and 1A complex · the same entry in another collection · chain A against A, TM-score 1.00
- P39730 · AlphaFold monomer V2.0 prediction for eukaryotic translation initiation factor 5B (P39730) · a predicted model of the same protein · chain A against A, TM-score 0.71
- P38912 · AlphaFold monomer V2.0 prediction for eukaryotic translation initiation factor 1A (P38912) · a predicted model of the same protein · chain C against A, TM-score 0.35
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 P39730
- Every structure of UniProt P38912
- Elsewhere: RCSB PDB 3WBK · PDBe 3WBK · UniProt P39730 · UniProt P38912
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