Research workbench
Crystal structure of the AG(I) form of E. COLI cuer, a copper efflux regulator
Analyse Crystal structure of the AG(I) form of E. COLI cuer, a copper efflux regulator in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1Q06
- Type
- protein
- Length
- 248 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Transcriptional regulator cuer
- UniProt
- P0A9G4
- Ligands
- AG
Structure
x-ray diffraction · 2 distinct chains · 68% helix, 3% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Transcriptional regulator cuer | protein | 122 | 69% helix, 3% strand | P0A9G4 |
| B | Transcriptional regulator cuer | protein | 126 | 67% helix, 3% strand | P0A9G4 |
Ligands and binding sites
- AG · Silver ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–B · 1949 Ų buried · 16 hydrogen bonds · protein-protein
Compared structures
- 1Q06 · Crystal structure of the Ag(I) form of E. coli CueR, a copper efflux regulator · the same entry in another collection · chain A against A, TM-score 1.00
- P0A9G4 · AlphaFold monomer V2.0 prediction for hth-type transcriptional regulator cuer (P0A9G4) · a predicted model of the same protein · chain B 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 P0A9G4
- Elsewhere: RCSB PDB 1Q06 · PDBe 1Q06 · UniProt P0A9G4
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