Research workbench
Structure of cnrh in complex with the cytosolic domain of cnry
Analyse Structure of cnrh in complex with the cytosolic domain of cnry in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4CXF
- Type
- protein
- Length
- 183 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- RNA polymerase sigma factor cnrh; Cnry
- UniProt
- P37978, P56621
- Ligands
- SO4, CL
Structure
x-ray diffraction · 2 distinct chains · 77% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | RNA polymerase sigma factor cnrh | protein | 154 | 79% helix, 0% strand | P37978 |
| B | Cnry | protein | 29 | 69% helix, 0% strand | P56621 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–B · 1226 Ų buried · 12 hydrogen bonds · protein-protein
Compared structures
- 4CXF · Structure of CnrH in complex with the cytosolic domain of CnrY · the same entry in another collection · chain A against A, TM-score 1.00
- P37978 · AlphaFold monomer V2.0 prediction for RNA polymerase sigma factor cnrh (P37978) · a predicted model of the same protein · chain A against A, TM-score 0.96
- P56621 · AlphaFold monomer V2.0 prediction for nickel and cobalt resistance protein cnry (P56621) · a predicted model of the same protein · chain B against A, TM-score 0.61
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 P37978
- Every structure of UniProt P56621
- Elsewhere: RCSB PDB 4CXF · PDBe 4CXF · UniProt P37978 · UniProt P56621
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