Research workbench
Homoserine transacetylase metx from mycobacterium hassiacum
Analyse Homoserine transacetylase metx from mycobacterium hassiacum in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5W8O
- Type
- protein
- Length
- 687 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Homoserine O-acetyltransferase
- EC
- 2.3.1.31
- UniProt
- K5B926
- Ligands
- CA, NA
- Pockets
- 6 · best druggability 0.67
Structure
x-ray diffraction · 2 distinct chains · 41% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Homoserine O-acetyltransferase (EC 2.3.1.31) | protein | 341 | 41% helix, 19% strand | K5B926 |
| B | Homoserine O-acetyltransferase (EC 2.3.1.31) | protein | 346 | 41% helix, 18% strand | K5B926 |
Ligands and binding sites
- CA · Calcium ion · metal · 4 copies · chains A, B
- NA · Sodium ion · metal · 2 copies · chains A, B
- GOL · Glycerol · additive · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 302 | 0.67 | 0.82 | 34 | empty |
| 2 | 254 | 0.62 | 0.81 | 37 | empty |
| 3 | 240 | 0.62 | 0.81 | 35 | empty |
| 4 | 270 | 0.59 | 0.79 | 43 | CA |
| 5 | 57 | 0.50 | 0.86 | 14 | empty |
Interfaces
1 interface between chains.
- A–B · 1768 Ų buried · 27 hydrogen bonds · protein-protein
Compared structures
- 5W8O · Homoserine transacetylase MetX from Mycobacterium hassiacum · 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 K5B926
- Elsewhere: RCSB PDB 5W8O · PDBe 5W8O · UniProt K5B926
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