Research workbench
Crystal structure of the DNA binding domain of arabidopsis thaliana auxin response factor 1, P21 structure
Analyse Crystal structure of the DNA binding domain of arabidopsis thaliana auxin… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4LDW
- Type
- protein
- Length
- 635 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Auxin response factor 1
- UniProt
- Q8L7G0
- Ligands
- CL
- Pockets
- 10 · best druggability 0.65
Structure
x-ray diffraction · 2 distinct chains · 21% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Auxin response factor 1 | protein | 311 | 21% helix, 30% strand | Q8L7G0 |
| B | Auxin response factor 1 | protein | 324 | 21% helix, 31% strand | Q8L7G0 |
Ligands and binding sites
- CL · Chloride ion · ion · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
10 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 338 | 0.65 | 0.80 | 45 | empty |
| 2 | 276 | 0.59 | 0.78 | 38 | empty |
| 3 | 202 | 0.54 | 0.79 | 32 | CL |
| 4 | 99 | 0.44 | 0.78 | 15 | empty |
| 5 | 133 | 0.42 | 0.75 | 18 | empty |
Interfaces
1 interface between chains.
- A–B · 944 Ų buried · 8 hydrogen bonds · protein-protein
Compared structures
- 4LDW · Crystal structure of the DNA Binding Domain of arabidopsis thaliana auxin response factor… · the same entry in another collection · chain A against A, TM-score 1.00
- Q8L7G0 · AlphaFold monomer V2.0 prediction for auxin response factor 1 (Q8L7G0) · a predicted model of the same protein · chain A against A, TM-score 0.96
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 Q8L7G0
- Elsewhere: RCSB PDB 4LDW · PDBe 4LDW · UniProt Q8L7G0
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