Research workbench
AlphaFold monomer V2.0 prediction for phosphocarrier protein hpr (P42013)
Analyse AlphaFold monomer V2.0 prediction for phosphocarrier protein hpr (P42013) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P42013
- Type
- protein
- Length
- 88 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xc0F878C3f3E2a1874e2A6daC80d429e553DdB0D5
- Molecule
- Phosphocarrier protein hpr
- UniProt
- P42013
Structure
1 distinct chain · 35% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phosphocarrier protein hpr | protein | 88 | 35% helix, 28% strand | P42013 |
Compared structures
- 1Y51 · X-ray crystal structure of Bacillus stearothermophilus Histidine phosphocarrier protein… · an experimental structure of the same protein · chain A against A, TM-score 0.98
- 1Y51 · X-ray crystal structure of bacillus stearothermophilus histidine phosphocarrier protein… · an experimental structure of the same protein · chain A against A, TM-score 0.98
- 1Y4Y · X-ray crystal structure of Bacillus stearothermophilus Histidine phosphocarrier protein… · an experimental structure of the same protein · chain A against A, TM-score 0.98
- 1Y4Y · X-ray crystal structure of bacillus stearothermophilus histidine phosphocarrier protein… · an experimental structure of the same protein · chain A against A, TM-score 0.98
- 1Y50 · X-ray crystal structure of Bacillus stearothermophilus Histidine phosphocarrier protein… · an experimental structure of the same protein · chain A against A, TM-score 0.56
- 1Y50 · X-ray crystal structure of bacillus stearothermophilus histidine phosphocarrier protein… · an experimental structure of the same protein · chain A against A, TM-score 0.56
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 P42013
- Elsewhere: UniProt P42013 · AlphaFold DB P42013
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