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Structural basis of dimerization and sensory mechanisms of oxygen- sensing domain of rhizobium meliloti fixl determined at 1.4A resolution
Analyse Structural basis of dimerization and sensory mechanisms of oxygen- sensing… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1D06
- Type
- protein
- Length
- 130 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P10955
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 130 | — | P10955 |
Compared structures
- 1D06 · Structural basis of dimerization and sensory mechanisms of oxygen-sensing domain of… · the same entry in another collection · chain A against A, TM-score 1.00
- P10955 · AlphaFold monomer V2.0 prediction for sensor protein fixl (P10955) · a predicted model of the same protein · chain A against A, TM-score 0.86
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 P10955
- Elsewhere: RCSB PDB 1D06 · PDBe 1D06 · UniProt P10955
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