Research workbench
Crystal structure of a putative N-acetyltransferase (TA0374) from thermoplasma acidophilum
Analyse Crystal structure of a putative N-acetyltransferase (TA0374) from thermoplasma… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3FIX
- Type
- protein
- Length
- 644 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- N-acetyltransferase
- UniProt
- Q9HL57
- Pockets
- 7 · best druggability 0.70
Structure
x-ray diffraction · 2 distinct chains · 43% helix, 32% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | N-acetyltransferase | protein | 165 | 44% helix, 32% strand | Q9HL57 |
| B, D | N-acetyltransferase | protein | 157 | 43% helix, 32% strand | Q9HL57 |
Ligands and binding sites
- EDO · 1,2-ethanediol · additive · 2 copies · chains A, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 698 | 0.70 | 0.77 | 63 | empty |
| 2 | 391 | 0.68 | 0.80 | 35 | EDO |
| 3 | 589 | 0.67 | 0.77 | 46 | empty |
| 4 | 407 | 0.67 | 0.80 | 33 | EDO |
| 5 | 337 | 0.60 | 0.77 | 28 | empty |
Interfaces
4 interfaces between chains.
- B–C · 425 Ų buried · 2 hydrogen bonds · protein-protein
- C–D · 351 Ų buried · 1 hydrogen bond · protein-protein
- A–B · 347 Ų buried · 1 hydrogen bond · protein-protein
- A–C · 61 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 10 modified (engineered).
Compared structures
- 3FIX · Crystal structure of a putative n-acetyltransferase (ta0374) from thermoplasma acidophilum · the same entry in another collection · chain A against A, TM-score 1.00
- Q9HL57 · AlphaFold monomer V2.0 prediction for spermidine N(1)-acetyltransferase (Q9HL57) · a predicted model of the same protein · chain A against A, TM-score 0.91
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 Q9HL57
- Elsewhere: RCSB PDB 3FIX · PDBe 3FIX · UniProt Q9HL57
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