Research workbench
Structure of human ALDH7A1 complexed with NAD+ in space group P4212
Analyse Structure of human ALDH7A1 complexed with NAD+ in space group P4212 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4ZVY
- Type
- protein
- Length
- 946 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Alpha-aminoadipic semialdehyde dehydrogenase
- EC
- 1.2.1.31, 1.2.1.3, 1.2.1.8
- UniProt
- P49419
- Ligands
- NAD
- Pockets
- 9 · best druggability 0.73
Structure
x-ray diffraction · 2 distinct chains · 44% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Alpha-aminoadipic semialdehyde dehydrogenase (EC 1.2.1.31, 1.2.1.3, 1.2.1.8) | protein | 472 | 44% helix, 22% strand | P49419 |
| B | Alpha-aminoadipic semialdehyde dehydrogenase (EC 1.2.1.31, 1.2.1.3, 1.2.1.8) | protein | 474 | 44% helix, 22% strand | P49419 |
Ligands and binding sites
- NAD · Nicotinamide-adenine-dinucleotide · ligand · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
9 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 739 | 0.73 | 0.79 | 85 | empty |
| 2 | 280 | 0.56 | 0.76 | 38 | NAD |
| 3 | 285 | 0.54 | 0.75 | 39 | empty |
| 4 | 68 | 0.53 | 0.87 | 23 | empty |
| 5 | 166 | 0.53 | 0.79 | 25 | empty |
Interfaces
1 interface between chains.
- A–B · 1749 Ų buried · 30 hydrogen bonds · protein-protein
Compared structures
- 4ZVY · Structure of human ALDH7A1 complexed with NAD+ in space group P4212 · the same entry in another collection · chain A against A, TM-score 1.00
- P49419 · AlphaFold monomer V2.0 prediction for alpha-aminoadipic semialdehyde dehydrogenase… · a predicted model of the same protein · chain A against A, TM-score 0.99
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 P49419
- Elsewhere: RCSB PDB 4ZVY · PDBe 4ZVY · UniProt P49419
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.