Research workbench
Crystal structure of a putative acetyltransferase (NP_394282.1) from thermoplasma acidophilum at 2.00 a resolution
Analyse Crystal structure of a putative acetyltransferase (NP_394282.1) from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3C26
- Type
- protein
- Length
- 257 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Putative acetyltransferase TA0821
- UniProt
- Q9HJZ0
- Ligands
- NO3
- Pockets
- 1 · best druggability 0.79
Structure
x-ray diffraction · 1 distinct chain · 31% helix, 39% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Putative acetyltransferase TA0821 | protein | 257 | 31% helix, 39% strand | Q9HJZ0 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 257 | 0.79 | 0.91 | 43 | NO3, EDO |
Modifications
Observed in the structure: 7 modified, 1 disulfide (engineered, disulfide).
Compared structures
- 3C26 · Crystal structure of a putative acetyltransferase (NP_394282.1) from Thermoplasma… · 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 Q9HJZ0
- Elsewhere: RCSB PDB 3C26 · PDBe 3C26 · UniProt Q9HJZ0
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