Research workbench
Crystal structure of human aminoadipate semialdehyde synthase, saccharopine dehydrogenase domain with N-[(2S)-2-Pyrrolidinylmethyl]-trifluoromethanesulfonamide bound
Analyse Crystal structure of human aminoadipate semialdehyde synthase, saccharopine… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5O1N
- Type
- protein
- Length
- 442 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.28
- Source
- Homo sapiens
- Molecule
- Alpha-aminoadipic semialdehyde synthase, mitochondrial
- EC
- 1.5.1.8, 1.5.1.9
- UniProt
- Q9UDR5
- Ligands
- 9H8
- Pockets
- 2 · best druggability 0.74
Structure
x-ray diffraction · resolution 2.28 · 1 distinct chain · 39% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Alpha-aminoadipic semialdehyde synthase, mitochondrial (EC 1.5.1.8, 1.5.1.9) | protein | 442 | 39% helix, 24% strand | Q9UDR5 |
Ligands and binding sites
- 9H8 · 1,1,1-tris(fluoranyl)-~{N}-[[(2~{S})-pyrrolidin-2-yl]methyl]methanesulfonamide · ligand · chains A
- DMS · Dimethyl sulfoxide · additive · chains A
- EDO · 1,2-ethanediol · additive · chains A
- PEG · Di(hydroxyethyl)ether · additive · 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, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 718 | 0.74 | 0.79 | 60 | 9H8, DMS, PEG |
| 2 | 127 | 0.45 | 0.77 | 20 | empty |
Compared structures
- 5O1N · Crystal structure of human aminoadipate semialdehyde synthase, saccharopine dehydrogenase… · the same entry in another collection · chain A against A, TM-score 1.00
- Q9UDR5 · AlphaFold monomer V2.0 prediction for alpha-aminoadipic semialdehyde synthase… · a predicted model of the same protein · chain A against A, TM-score 0.97
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 Q9UDR5
- Elsewhere: RCSB PDB 5O1N · PDBe 5O1N · UniProt Q9UDR5
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.