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Structure of the bacterial replication origin-associated protein cnu
Analyse Structure of the bacterial replication origin-associated protein cnu in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2JQT
- Type
- protein
- Length
- 57 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- H-NS/STPA-binding protein 2
- UniProt
- P64467
Structure
solution nmr · 1 distinct chain · 67% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | H-NS/STPA-binding protein 2 | protein | 57 | 67% helix, 0% strand | P64467 |
Compared structures
- 2JQT · Structure of the bacterial replication origin-associated protein Cnu · the same entry in another collection · chain A against A, TM-score 1.00
- P64467 · AlphaFold monomer V2.0 prediction for oric-binding nucleoid- associated protein (P64467) · a predicted model of the same protein · chain A against A, TM-score 0.71
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 P64467
- Elsewhere: RCSB PDB 2JQT · PDBe 2JQT · UniProt P64467
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