Research workbench
Crystal structure of escherichia COLI aspartate beta-semialdehyde dehydrogenase (ecasadh), at 1.95 ångström resolution
Analyse Crystal structure of escherichia COLI aspartate beta-semialdehyde dehydrogenase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1T4D
- Type
- protein
- Length
- 1,101 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Aspartate-semialdehyde dehydrogenase
- EC
- 1.2.1.11
- UniProt
- P0A9Q9
- Pockets
- 6 · best druggability 0.62
Structure
x-ray diffraction · 1 distinct chain · 40% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | Aspartate-semialdehyde dehydrogenase (EC 1.2.1.11) | protein | 367 | 40% helix, 22% strand | P0A9Q9 |
Pockets
6 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 419 | 0.62 | 0.77 | 37 | empty |
| 2 | 391 | 0.61 | 0.77 | 50 | empty |
| 3 | 350 | 0.60 | 0.77 | 41 | empty |
| 4 | 303 | 0.55 | 0.76 | 38 | empty |
| 5 | 75 | 0.31 | 0.74 | 16 | empty |
Interfaces
3 interfaces between chains.
- A–B · 3613 Ų buried · 52 hydrogen bonds · protein-protein
- A–C · 238 Ų buried · 3 hydrogen bonds · protein-protein
- B–C · 183 Ų buried · 3 hydrogen bonds · protein-protein
Compared structures
- 1T4D · Crystal structure of Escherichia coli aspartate beta-semialdehyde dehydrogenase… · the same entry in another collection · chain A against A, TM-score 1.00
- P0A9Q9 · AlphaFold monomer V2.0 prediction for aspartate-semialdehyde dehydrogenase (P0A9Q9) · a predicted model of the same protein · 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 P0A9Q9
- Elsewhere: RCSB PDB 1T4D · PDBe 1T4D · UniProt P0A9Q9
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