Research workbench
SE-DBD
Analyse SE-DBD in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7E1D
- Type
- protein
- Length
- 189 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- DNA-binding response regulator
- UniProt
- A0A0L8SKF9
Structure
x-ray diffraction · 2 distinct chains · 36% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B | DNA-binding response regulator | protein | 94 | 36% helix, 26% strand | A0A0L8SKF9 |
| A | DNA-binding response regulator | protein | 95 | 36% helix, 27% strand | A0A0L8SKF9 |
Interfaces
1 interface between chains.
- B–A · 2366 Ų buried · 21 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 modified (engineered).
Compared structures
- 7E1D · Se-DBD · the same entry in another collection · chain B against B, 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 A0A0L8SKF9
- Elsewhere: RCSB PDB 7E1D · PDBe 7E1D · UniProt A0A0L8SKF9
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