Research workbench
Structure of ALDH7A1 mutant W175A complexed with NAD
Analyse Structure of ALDH7A1 mutant W175A complexed with NAD in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6O4C
- Type
- protein
- Length
- 4,072 residues
- Chains
- 8
- 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, MG, CL
- Pockets
- 20 · best druggability 0.87
Structure
x-ray diffraction · 1 distinct chain · 41% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G, H | Alpha-aminoadipic semialdehyde dehydrogenase (EC 1.2.1.31, 1.2.1.3, 1.2.1.8) | protein | 509 | 41% helix, 21% strand | P49419 |
Ligands and binding sites
- NAD · Nicotinamide-adenine-dinucleotide · ligand · 8 copies · chains A, B, C, D, E, F, G, H
- MG · Magnesium ion · metal · 3 copies
- CL · Chloride ion · ion · 8 copies · chains A, B, C, D, E, F, G, H
- PGE · Triethylene glycol · additive · 8 copies · chains A, B, C, D, E, F, G, H
- 1PE · Pentaethylene glycol · additive · 8 copies · chains A, B, C, D, E, F, G, H
- EDO · 1,2-ethanediol · additive · 7 copies · chains C, B, D, E, F, H, G
- PEG · Di(hydroxyethyl)ether · additive · chains E
- PG4 · Tetraethylene glycol · additive · chains H
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 | 1116 | 0.87 | 0.88 | 87 | 1PE |
| 2 | 1141 | 0.87 | 0.88 | 88 | 1PE |
| 3 | 1130 | 0.87 | 0.88 | 87 | 1PE |
| 4 | 1167 | 0.87 | 0.88 | 87 | 1PE |
| 5 | 1159 | 0.85 | 0.87 | 70 | EDO |
Interfaces
16 interfaces between chains.
- E–F · 4011 Ų buried · 63 hydrogen bonds · protein-protein
- G–H · 4002 Ų buried · 65 hydrogen bonds · protein-protein
- A–B · 3990 Ų buried · 66 hydrogen bonds · protein-protein
- C–D · 3966 Ų buried · 67 hydrogen bonds · protein-protein
- E–G · 984 Ų buried · 3 hydrogen bonds · protein-protein
Compared structures
- 6O4C · Structure of ALDH7A1 mutant W175A complexed with NAD · the same entry in another collection · chain F against F, TM-score 1.00
- P49419 · AlphaFold monomer V2.0 prediction for alpha-aminoadipic semialdehyde dehydrogenase… · a predicted model of the same protein · chain G 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 P49419
- Elsewhere: RCSB PDB 6O4C · PDBe 6O4C · UniProt P49419
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