MolNFT v1 · #157379 · protein
The crystal structure of the regulatory domain of aspartokinase in the bifunctional ASPARTOKINASE/HOMOSERINE dehydrogenase 1 from escherichia COLI str. K-12 substr. MG1655
6MX1: “The crystal structure of the regulatory domain of aspartokinase in the bifunctional ASPARTOKINASE/HOMOSERINE…”. X-ray diffraction, 3 pockets (best druggability 0.62). MolNFT v1 #157379 on GenesisL1: 3D structure, binding sites and…
- PDB
- 6MX1
- Type
- protein
- Length
- 311 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Bifunctional ASPARTOKINASE/HOMOSERINE dehydrogenase 1
- EC
- 2.7.2.4, 1.1.1.3
- UniProt
- P00561
- Pockets
- 3 · best druggability 0.62
Structure
x-ray diffraction · 2 distinct chains · 40% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Bifunctional ASPARTOKINASE/HOMOSERINE dehydrogenase 1 (EC 2.7.2.4, 1.1.1.3) | protein | 156 | 38% helix, 31% strand | P00561 |
| B | Bifunctional ASPARTOKINASE/HOMOSERINE dehydrogenase 1 (EC 2.7.2.4, 1.1.1.3) | protein | 155 | 41% helix, 30% strand | P00561 |
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 104 | 0.62 | 0.88 | 20 | empty |
| 2 | 98 | 0.60 | 0.87 | 20 | empty |
| 3 | 79 | 0.44 | 0.80 | 22 | empty |
Interfaces
1 interface between chains.
- A–B · 1903 Ų buried · 37 hydrogen bonds · protein-protein
Compared structures
- 6MX1 · The crystal structure of the regulatory domain of aspartokinase in the bifunctional… · the same entry in another collection · chain A against A, TM-score 1.00
- P00561 · AlphaFold monomer V2.0 prediction for bifunctional ASPARTOKINASE/HOMOSERINE dehydrogenase… · a predicted model of the same protein · chain B against A, TM-score 0.96
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 P00561
- Elsewhere: RCSB PDB 6MX1 · PDBe 6MX1 · UniProt P00561
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