Research workbench
Solution structure of MDA5 ctd
Analyse Solution structure of MDA5 ctd in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2RQB
- Type
- protein
- Length
- 135 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Interferon-induced helicase C domain-containing protein 1
- EC
- 3.6.1.-
- UniProt
- Q9BYX4
- Ligands
- ZN
- Pockets
- 2 · best druggability 0.40
Structure
solution nmr · 1 distinct chain · 10% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Interferon-induced helicase C domain-containing protein 1 (EC 3.6.1.-) | protein | 135 | 10% helix, 29% strand | Q9BYX4 |
Ligands and binding sites
- ZN · Zinc ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 73 | 0.40 | 0.79 | 23 | empty |
| 2 | 56 | 0.32 | 0.77 | 16 | empty |
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
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 Q9BYX4
- Elsewhere: RCSB PDB 2RQB · PDBe 2RQB · UniProt Q9BYX4
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