MolNFT v1 · #138110 · protein
Homoserine transacetylase metx from mycobacterium abscessus
5W8P · Homoserine O-acetyltransferase: “Homoserine transacetylase metx from mycobacterium abscessus”. X-ray diffraction, 2 ligands (K, PO4), 7 pockets (best druggability 0.67). MolNFT v1 #138110 on GenesisL1: 3D structure, binding sites…
- PDB
- 5W8P
- Type
- protein
- Length
- 739 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
- B1MG17
- Ligands
- K, PO4
- Pockets
- 7 · best druggability 0.67
Structure
x-ray diffraction · 2 distinct chains · 37% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Homoserine O-acetyltransferase (EC 2.3.1.31) | protein | 370 | 37% helix, 19% strand | B1MG17 |
| B | Homoserine O-acetyltransferase (EC 2.3.1.31) | protein | 369 | 37% helix, 19% strand | B1MG17 |
Ligands and binding sites
- K · Potassium ion · metal · 2 copies · chains A, B
- PO4 · Phosphate ion · ion · 6 copies · chains A, B
- GOL · Glycerol · additive · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 320 | 0.67 | 0.82 | 37 | empty |
| 2 | 283 | 0.64 | 0.81 | 34 | empty |
| 3 | 263 | 0.60 | 0.80 | 26 | empty |
| 4 | 64 | 0.52 | 0.87 | 22 | empty |
| 5 | 193 | 0.51 | 0.77 | 35 | empty |
Interfaces
1 interface between chains.
- A–B · 1884 Ų buried · 25 hydrogen bonds · protein-protein
Compared structures
- 5W8P · Homoserine transacetylase MetX from Mycobacterium abscessus · 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 B1MG17
- Elsewhere: RCSB PDB 5W8P · PDBe 5W8P · UniProt B1MG17
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