MolNFT v1 · #115056 · protein
Crystal structure of ARD1 N-terminal acetyltransferase from sulfolobus solfataricus in monoclinic form
5C88 · Uncharacterized N-acetyltransferase SSO0209: “Crystal structure of ARD1 N-terminal acetyltransferase from sulfolobus solfataricus in monoclinic form”. X-ray diffraction, 1 ligand (COA), 2 pockets (best druggability 0.68). MolNFT v1…
- PDB
- 5C88
- Type
- protein
- Length
- 315 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Uncharacterized N-acetyltransferase SSO0209
- EC
- 2.3.1.88
- UniProt
- Q980R9
- Ligands
- COA
- Pockets
- 2 · best druggability 0.68
Structure
x-ray diffraction · 2 distinct chains · 33% helix, 35% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Uncharacterized N-acetyltransferase SSO0209 (EC 2.3.1.88) | protein | 158 | 32% helix, 35% strand | Q980R9 |
| B | Uncharacterized N-acetyltransferase SSO0209 (EC 2.3.1.88) | protein | 157 | 34% helix, 35% strand | Q980R9 |
Ligands and binding sites
- COA · Coenzyme A · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 414 | 0.68 | 0.80 | 36 | COA |
| 2 | 287 | 0.62 | 0.79 | 35 | COA |
Interfaces
1 interface between chains.
- A–B · 601 Ų buried · 8 hydrogen bonds · protein-protein
Compared structures
- 5C88 · Crystal structure of Ard1 N-terminal acetyltransferase from Sulfolobus solfataricus in… · 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 B 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 5C88 · PDBe 5C88 · UniProt Q980R9
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