Research workbench
Crystal structure of ARD1 N-terminal acetyltransferase E88H/H127E mutant from sulfolobus solfataricus
Analyse Crystal structure of ARD1 N-terminal acetyltransferase E88H/H127E mutant from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6AG5
- Type
- protein
- Length
- 157 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- N-alpha-acetyltransferase
- EC
- 2.3.1.255, 2.3.1.258
- UniProt
- Q980R9
- Ligands
- ACO, CA
- Pockets
- 1 · best druggability 0.63
Structure
x-ray diffraction · 1 distinct chain · 35% helix, 34% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | N-alpha-acetyltransferase (EC 2.3.1.255, 2.3.1.258) | protein | 157 | 35% helix, 34% strand | Q980R9 |
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 | 305 | 0.63 | 0.80 | 33 | ACO, CA |
Compared structures
- 6AG5 · Crystal structure of Ard1 N-terminal acetyltransferase E88H/H127E mutant from Sulfolobus… · the same entry in another collection · chain A against A, TM-score 1.00
- Q980R9 · AlphaFold monomer V2.0 prediction for N-alpha-acetyltransferase (Q980R9) · a predicted model of the same protein · chain A against A, TM-score 0.98
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 Q980R9
- Elsewhere: RCSB PDB 6AG5 · PDBe 6AG5 · UniProt Q980R9
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