Research workbench
Crystal structure of L-serine-O-acetyltransferase found in D- cycloserine biosynthetic pathway
Analyse Crystal structure of L-serine-O-acetyltransferase found in D- cycloserine… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3VVL
- Type
- protein
- Length
- 737 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
- D2Z028
- Pockets
- 9 · best druggability 0.71
Structure
x-ray diffraction · 2 distinct chains · 39% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Homoserine O-acetyltransferase (EC 2.3.1.31) | protein | 368 | 40% helix, 18% strand | D2Z028 |
| B | Homoserine O-acetyltransferase (EC 2.3.1.31) | protein | 369 | 39% helix, 18% strand | D2Z028 |
Pockets
9 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 444 | 0.71 | 0.81 | 48 | empty |
| 2 | 435 | 0.69 | 0.80 | 45 | empty |
| 3 | 77 | 0.64 | 0.92 | 24 | empty |
| 4 | 213 | 0.56 | 0.79 | 34 | empty |
| 5 | 82 | 0.47 | 0.81 | 18 | empty |
Interfaces
1 interface between chains.
- A–B · 2193 Ų buried · 35 hydrogen bonds · protein-protein
Compared structures
- 3VVL · Crystal structure of L-serine-O-acetyltransferase found in D-cycloserine biosynthetic… · the same entry in another collection · chain A against A, TM-score 1.00
- D2Z028 · AlphaFold monomer V2.0 prediction for L-SERINE/HOMOSERINE O-acetyltransferase (D2Z028) · a predicted model of the same protein · 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 D2Z028
- Elsewhere: RCSB PDB 3VVL · PDBe 3VVL · UniProt D2Z028
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