MolNFT v2 · #180038 · protein
The cryo-EM structure of the DDX42-SF3b complex
7EVN: “The cryo-EM structure of the DDX42-SF3b complex”. Electron microscopy at 2.6, 1 ligand (ZN). MolNFT v2 #180038 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 7EVN
- Type
- protein
- Length
- 2,649 residues
- Chains
- 5
- Method
- electron microscopy
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.6
- Source
- Homo sapiens
- UniProt
- Q9BWJ5, O75533, Q7RTV0, Q15393, Q86XP3
- Ligands
- ZN
Structure
electron microscopy · resolution 2.6 · 5 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B | — | protein | 78 | — | Q9BWJ5 |
| C | — | protein | 815 | — | O75533 |
| D | — | protein | 93 | — | Q7RTV0 |
| A | — | protein | 1177 | — | Q15393 |
| E | — | protein | 486 | — | Q86XP3 |
Ligands and binding sites
- ZN · Zinc ion · metal · 3 copies · chains D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7EVN · The cryo-EM structure of the DDX42-SF3B complex · the same entry in another collection · chain B against B, TM-score 1.00
- Q15393 · AlphaFold monomer V2.0 prediction for splicing factor 3B subunit 3 (Q15393) · a predicted model of the same protein · chain A against A, TM-score 0.96
- Q86XP3 · AlphaFold monomer V2.0 prediction for ATP-dependent RNA helicase DDX42 (Q86XP3) · a predicted model of the same protein · chain E against A, TM-score 0.54
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 Q9BWJ5
- Every structure of UniProt O75533
- Every structure of UniProt Q7RTV0
- Every structure of UniProt Q15393
- Every structure of UniProt Q86XP3
- Elsewhere: RCSB PDB 7EVN · PDBe 7EVN · UniProt Q9BWJ5 · UniProt O75533 · UniProt Q7RTV0 · UniProt Q15393 · UniProt Q86XP3
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