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Structural flexibility in region involved in dimer formation of nuclease domain of ribonuclase III (rnc) from campylobacter jejuni
Analyse Structural flexibility in region involved in dimer formation of nuclease domain… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3O2R
- Type
- protein
- Length
- 574 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- D3FPA5
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | — | protein | 144 | — | D3FPA5 |
| B, D | — | protein | 143 | — | D3FPA5 |
Compared structures
- 3O2R · Structural flexibility in region involved in dimer formation of nuclease domain of… · the same entry in another collection · 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 D3FPA5
- Elsewhere: RCSB PDB 3O2R · PDBe 3O2R · UniProt D3FPA5
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