Research workbench
The crystal structure of the DPS2 from deinococcus radiodurans to 1.83A resolution (sequentially soaked in CACL2 [5MM] for 20 min, then in ammonium IRON(II) sulfate [10MM] for 2H).
Analyse The crystal structure of the DPS2 from deinococcus radiodurans to 1.83A… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6TB5
- Type
- protein
- Length
- 165 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- DNA protection during starvation protein 2
- EC
- 1.16.-.-
- UniProt
- Q9RZN1
- Ligands
- FE, CA
Structure
x-ray diffraction · 1 distinct chain · 72% helix, 4% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | DNA protection during starvation protein 2 (EC 1.16.-.-) | protein | 165 | 72% helix, 4% strand | Q9RZN1 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6TB5 · The crystal structure of the DPS2 from DEINOCOCCUS RADIODURANS to 1.83A resolution… · the same entry in another collection · chain A against A, TM-score 1.00
- Q9RZN1 · AlphaFold monomer V2.0 prediction for DNA protection during starvation protein 2 (Q9RZN1) · a predicted model of the same protein · 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 Q9RZN1
- Elsewhere: RCSB PDB 6TB5 · PDBe 6TB5 · UniProt Q9RZN1
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