Research workbench
Crystal structure of ARD1 N-terminal acetyltransferase H88A/E127A mutant from sulfolobus solfataricus
Analyse Crystal structure of ARD1 N-terminal acetyltransferase H88A/E127A mutant from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6AG4
- Type
- protein
- Length
- 157 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q980R9
- Ligands
- ACO, CA, SO4
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 157 | — | Q980R9 |
Ligands and binding sites
- ACO · Acetyl coenzyme *A · ligand · chains A
- CA · Calcium ion · metal · chains A
- SO4 · Sulfate ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6AG4 · Crystal structure of Ard1 N-terminal acetyltransferase H88A/E127A 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 0.99
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 6AG4 · PDBe 6AG4 · UniProt Q980R9
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.