Research workbench
IRED-88
Analyse IRED-88 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7OG3
- Type
- protein
- Length
- 580 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- NAD(P)-dependent oxidoreductase
- UniProt
- A0A5P2XKZ4
- Ligands
- NDP, NA
- Pockets
- 3 · best druggability 0.75
Structure
x-ray diffraction · 1 distinct chain · 59% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | NAD(P)-dependent oxidoreductase | protein | 290 | 59% helix, 12% strand | A0A5P2XKZ4 |
Ligands and binding sites
- NDP · Nadph dihydro-nicotinamide-adenine-dinucleotide phosphate · ligand · 2 copies · chains A, B
- NA · Sodium ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 670 | 0.75 | 0.81 | 55 | NDP |
| 2 | 703 | 0.75 | 0.80 | 59 | NDP |
| 3 | 81 | 0.66 | 0.91 | 22 | empty |
Interfaces
1 interface between chains.
- A–B · 4734 Ų buried · 43 hydrogen bonds · protein-protein
Compared structures
- 7OG3 · IRED-88 · 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 A0A5P2XKZ4
- Elsewhere: RCSB PDB 7OG3 · PDBe 7OG3 · UniProt A0A5P2XKZ4
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