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Crystal structure of a selenomethionine-substituted A70M I84M mutant of the essential repressor ddro from radiation resistant-deinococcus bacteria (deinococcus deserti)
Analyse Crystal structure of a selenomethionine-substituted A70M I84M mutant of the… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6RMQ
- Type
- protein
- Length
- 244 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hth-type transcriptional regulator ddroc
- UniProt
- C1CYP4
Structure
x-ray diffraction · 1 distinct chain · 57% helix, 2% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Hth-type transcriptional regulator ddroc | protein | 122 | 57% helix, 2% strand | C1CYP4 |
Interfaces
1 interface between chains.
- A–B · 1630 Ų buried · 9 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 modified (engineered).
Compared structures
- 6RMQ · Crystal structure of a selenomethionine-substituted A70M I84M mutant of the essential… · the same entry in another collection · chain A against A, TM-score 1.00
- C1CYP4 · AlphaFold monomer V2.0 prediction for hth-type transcriptional regulator ddroc (C1CYP4) · a predicted model of the same protein · chain A against A, TM-score 0.61
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 C1CYP4
- Elsewhere: RCSB PDB 6RMQ · PDBe 6RMQ · UniProt C1CYP4
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