Research workbench
Restored heptad pattern continuity does not alter the folding of a 4- alpha-helical bundle
Analyse Restored heptad pattern continuity does not alter the folding of a 4… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1RPO
- Type
- protein
- Length
- 61 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Rop protein
- UniProt
- P03051
Structure
x-ray diffraction · 1 distinct chain · 90% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Rop protein | protein | 61 | 90% helix, 0% strand | P03051 |
Compared structures
- 1RPO · Restored heptad pattern continuity does not alter the folding of a 4-alpha-helical bundle · the same entry in another collection · chain A against A, TM-score 1.00
- P03051 · AlphaFold monomer V2.0 prediction for regulatory protein rop (P03051) · a predicted model of the same protein · chain A against A, TM-score 0.89
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 P03051
- Elsewhere: RCSB PDB 1RPO · PDBe 1RPO · UniProt P03051
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