Research workbench
The myristoylated yeast ARF1 in a GTP and bicelle bound conformation
Analyse The myristoylated yeast ARF1 in a GTP and bicelle bound conformation in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2KSQ
- Type
- protein
- Length
- 180 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- ADP-ribosylation factor 1
- UniProt
- P11076
- Ligands
- MTN, MYR, GTP
- Pockets
- 2 · best druggability 0.41
Structure
solution nmr · 1 distinct chain · 36% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ADP-ribosylation factor 1 | protein | 180 | 36% helix, 23% strand | P11076 |
Ligands and binding sites
- MTN · S-[(1-oxyl-2,2,5,5-tetramethyl-2,5-dihydro-1H-pyrrol-3-yl)methyl] methanesulfonothioate · ligand · 5 copies · chains A
- MYR · Myristic acid · ligand · chains A
- GTP · Guanosine-5'-triphosphate · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 110 | 0.41 | 0.76 | 18 | empty |
| 2 | 61 | 0.34 | 0.77 | 22 | GTP |
Modifications
Observed in the structure: 5 covalent, 1 lipid (covalent ligand, myristoylation).
Compared structures
- 2KSQ · The myristoylated yeast ARF1 in a GTP and bicelle bound conformation · the same entry in another collection · chain A against A, TM-score 1.00
- P11076 · AlphaFold monomer V2.0 prediction for ADP-ribosylation factor 1 (P11076) · a predicted model of the same protein · chain A against A, TM-score 0.84
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 P11076
- Elsewhere: RCSB PDB 2KSQ · PDBe 2KSQ · UniProt P11076
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