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Crystal structure of aspartate semialdehyde dehydrogenase from thermus thermophilus HB8
Analyse Crystal structure of aspartate semialdehyde dehydrogenase from thermus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2YV3
- Type
- protein
- Length
- 656 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
- Q5SKU8
- Pockets
- 8 · best druggability 0.58
Structure
x-ray diffraction · 1 distinct chain · 34% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Aspartate-semialdehyde dehydrogenase (EC 1.2.1.11) | protein | 328 | 34% helix, 24% strand | Q5SKU8 |
Pockets
8 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 331 | 0.58 | 0.77 | 40 | empty |
| 2 | 50 | 0.56 | 0.90 | 17 | empty |
| 3 | 238 | 0.52 | 0.76 | 32 | empty |
| 4 | 57 | 0.42 | 0.82 | 15 | empty |
| 5 | 57 | 0.36 | 0.79 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 2580 Ų buried · 38 hydrogen bonds · protein-protein
Compared structures
- 2YV3 · Crystal Structure of Aspartate Semialdehyde Dehydrogenase from Thermus thermophilus HB8 · 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 Q5SKU8
- Elsewhere: RCSB PDB 2YV3 · PDBe 2YV3 · UniProt Q5SKU8
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