Research workbench
Aspartate beta-semialdehyde dehydrogenase in complex with NADP and substrate analogue S-methyl cysteine sulfoxide
Analyse Aspartate beta-semialdehyde dehydrogenase in complex with NADP and substrate… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1GL3
- Type
- protein
- Length
- 734 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Aspartate-semialdehyde dehydrogenase
- EC
- 1.2.1.11
- UniProt
- P00353
- Ligands
- NDP, CYS
- Pockets
- 4 · best druggability 0.71
Structure
x-ray diffraction · 1 distinct chain · 40% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Aspartate-semialdehyde dehydrogenase (EC 1.2.1.11) | protein | 367 | 40% helix, 23% strand | P00353 |
Ligands and binding sites
- NDP · Nadph dihydro-nicotinamide-adenine-dinucleotide phosphate · ligand · 2 copies · chains A, B
- CYS · Cysteine · ligand · 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 | 626 | 0.71 | 0.79 | 71 | CYS, NDP |
| 2 | 665 | 0.70 | 0.78 | 78 | NDP |
| 3 | 63 | 0.35 | 0.78 | 15 | empty |
| 4 | 60 | 0.29 | 0.75 | 17 | empty |
Interfaces
1 interface between chains.
- A–B · 3842 Ų buried · 49 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 covalent (covalent ligand).
Compared structures
- 1GL3 · Aspartate beta-semialdehyde dehydrogenase in complex with NADP and substrate analogue… · 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 P00353
- Elsewhere: RCSB PDB 1GL3 · PDBe 1GL3 · UniProt P00353
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