Research workbench
REA1 wild type ADP state (aaa+ ring part)
Analyse REA1 wild type ADP state (aaa+ ring part) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6HYP
- Type
- protein
- Length
- 2,272 residues
- Chains
- 1
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- MIDASIN,MIDASIN
- UniProt
- Q12019
- Ligands
- ADP
- Pockets
- 20 · best druggability 0.84
Structure
electron microscopy · 1 distinct chain · 38% helix, 7% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | MIDASIN,MIDASIN | protein | 2272 | 38% helix, 7% strand | Q12019 |
Ligands and binding sites
- ADP · Adenosine-5'-diphosphate · ligand · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 708 | 0.84 | 0.88 | 109 | empty |
| 2 | 654 | 0.78 | 0.83 | 101 | empty |
| 3 | 374 | 0.78 | 0.87 | 55 | empty |
| 4 | 436 | 0.77 | 0.86 | 69 | empty |
| 5 | 534 | 0.76 | 0.83 | 76 | empty |
Compared structures
- 6HYP · Rea1 Wild type ADP state (AAA+ ring part) · the same entry in another collection · chain A against A, TM-score 1.00
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 Q12019
- Elsewhere: RCSB PDB 6HYP · PDBe 6HYP · UniProt Q12019
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