Research workbench
Structure of human ALDH1A1 with inhibitor CM039
Analyse Structure of human ALDH1A1 with inhibitor CM039 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5TEI
- Type
- protein
- Length
- 493 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Retinal dehydrogenase 1
- EC
- 1.2.1.36
- UniProt
- P00352
- Ligands
- NAI, M39, YB, CL
- Pockets
- 4 · best druggability 0.69
Structure
x-ray diffraction · 1 distinct chain · 42% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Retinal dehydrogenase 1 (EC 1.2.1.36) | protein | 493 | 42% helix, 22% strand | P00352 |
Ligands and binding sites
- NAI · 1,4-dihydronicotinamide adenine dinucleotide · ligand · chains A
- M39 · 6-{[(3-fluorophenyl)methyl]sulfanyl}-5-(2-methylphenyl)-2,5-dihydro-4H-pyrazolo[3,4-d]pyrimidin-4-one · ligand · chains A
- YB · Ytterbium (III) ion · metal · 2 copies · chains A
- CL · Chloride ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 372 | 0.69 | 0.82 | 44 | M39 |
| 2 | 304 | 0.64 | 0.80 | 38 | NAI, YB |
| 3 | 74 | 0.40 | 0.79 | 16 | empty |
| 4 | 100 | 0.37 | 0.75 | 16 | empty |
Compared structures
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 P00352
- Elsewhere: RCSB PDB 5TEI · PDBe 5TEI · UniProt P00352
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