Research workbench
Corynebacterium glutamicum hydrolyzed homoserine kinase
Analyse Corynebacterium glutamicum hydrolyzed homoserine kinase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5WAS
- Type
- protein
- Length
- 279 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Homoserine kinase
- EC
- 2.7.1.39
- UniProt
- P07128
- Ligands
- PO4
- Pockets
- 4 · best druggability 0.66
Structure
x-ray diffraction · 3 distinct chains · 28% helix, 34% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Homoserine kinase (EC 2.7.1.39) | protein | 180 | 26% helix, 36% strand | P07128 |
| B | Homoserine kinase (EC 2.7.1.39) | protein | 37 | 43% helix, 24% strand | P07128 |
| C | Homoserine kinase (EC 2.7.1.39) | protein | 62 | 24% helix, 32% strand | P07128 |
Ligands and binding sites
- PO4 · Phosphate 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 | 55 | 0.66 | 0.95 | 23 | empty |
| 2 | 155 | 0.51 | 0.79 | 21 | empty |
| 3 | 122 | 0.45 | 0.78 | 34 | PO4 |
| 4 | 55 | 0.28 | 0.74 | 12 | empty |
Interfaces
3 interfaces between chains.
- A–C · 1813 Ų buried · 36 hydrogen bonds · protein-protein
- A–B · 542 Ų buried · 5 hydrogen bonds · protein-protein
- B–C · 314 Ų buried · 3 hydrogen bonds · protein-protein
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 P07128
- Elsewhere: RCSB PDB 5WAS · PDBe 5WAS · UniProt P07128
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