Research workbench
A novel mode of rbd-protein recognition in the Y14-mago complex
Analyse A novel mode of rbd-protein recognition in the Y14-mago complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1HL6
- Type
- protein
- Length
- 510 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q9V535, P49028
Structure
x-ray diffraction · 4 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 119 | — | Q9V535 |
| B | — | protein | 137 | — | P49028 |
| C | — | protein | 111 | — | Q9V535 |
| D | — | protein | 143 | — | P49028 |
Compared structures
- 1HL6 · A novel mode of RBD-protein recognition in the Y14-mago complex · the same entry in another collection · chain D against D, TM-score 1.00
- P49028 · AlphaFold monomer V2.0 prediction for protein mago nashi (P49028) · a predicted model of the same protein · chain B against A, TM-score 0.96
- Q9V535 · AlphaFold monomer V2.0 prediction for RNA-binding protein 8A (Q9V535) · a predicted model of the same protein · chain C against A, TM-score 0.77
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 Q9V535
- Every structure of UniProt P49028
- Elsewhere: RCSB PDB 1HL6 · PDBe 1HL6 · UniProt Q9V535 · UniProt P49028
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