Research workbench
Crystal structure of TA0583, an archaeal actin homolog, complex with ADP
Analyse Crystal structure of TA0583, an archaeal actin homolog, complex with ADP in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2FSN
- Type
- protein
- Length
- 621 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hypothetical protein TA0583
- UniProt
- Q9HKL4
- Ligands
- ADP, MG
- Pockets
- 6 · best druggability 0.66
Structure
x-ray diffraction · 2 distinct chains · 37% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Hypothetical protein TA0583 | protein | 310 | 38% helix, 27% strand | Q9HKL4 |
| B | Hypothetical protein TA0583 | protein | 311 | 35% helix, 24% strand | Q9HKL4 |
Ligands and binding sites
- ADP · Adenosine-5'-diphosphate · ligand · 2 copies · chains A, B
- MG · Magnesium ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 369 | 0.66 | 0.80 | 47 | MG, ADP |
| 2 | 362 | 0.65 | 0.80 | 53 | MG, ADP |
| 3 | 73 | 0.48 | 0.83 | 24 | empty |
| 4 | 73 | 0.38 | 0.78 | 22 | empty |
| 5 | 69 | 0.35 | 0.77 | 18 | empty |
Interfaces
1 interface between chains.
- A–B · 148 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 10 modified (engineered).
Compared structures
- 2FSN · Crystal structure of Ta0583, an archaeal actin homolog, complex with ADP · the same entry in another collection · chain A against A, TM-score 1.00
- Q9HKL4 · AlphaFold monomer V2.0 prediction for archaeal actin homolog (Q9HKL4) · 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 Q9HKL4
- Elsewhere: RCSB PDB 2FSN · PDBe 2FSN · UniProt Q9HKL4
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