Research workbench
Structures of two arsr AS(III)-responsive repressors: implications for the mechanism of derepression
Analyse Structures of two arsr AS(III)-responsive repressors: implications for the… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6J05
- Type
- protein
- Length
- 191 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Transcriptional regulator arsr
- UniProt
- A0A2W1K2S1
- Ligands
- NA, ARS
Structure
x-ray diffraction · 2 distinct chains · 58% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Transcriptional regulator arsr | protein | 101 | 54% helix, 14% strand | A0A2W1K2S1 |
| B | Transcriptional regulator arsr | protein | 90 | 62% helix, 14% strand | A0A2W1K2S1 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–B · 1173 Ų buried · 9 hydrogen bonds · protein-protein
Compared structures
- 6J05 · Structures of two ArsR As(III)-responsive repressors: implications for the mechanism of… · the same entry in another collection · chain A against A, TM-score 1.00
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 A0A2W1K2S1
- Elsewhere: RCSB PDB 6J05 · PDBe 6J05 · UniProt A0A2W1K2S1
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