Research workbench
AlphaFold monomer V2.0 prediction for ribonuclease 4 (P34096)
Analyse AlphaFold monomer V2.0 prediction for ribonuclease 4 (P34096) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P34096
- Type
- protein
- Length
- 147 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xF65770DDF5857c17e162fAbC6d5BB9485dCED8ac
- Molecule
- Ribonuclease 4
- UniProt
- P34096
Structure
1 distinct chain · 33% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ribonuclease 4 | protein | 147 | 33% helix, 27% strand | P34096 |
Modifications
Observed in the structure: 4 disulfide (disulfide).
Compared structures
- 1RNF · X-ray crystal structure of unliganded human ribonuclease 4 · an experimental structure of the same protein · chain A against A, TM-score 0.81
- 1RNF · X-ray crystal structure of unliganded human ribonuclease 4 · an experimental structure of the same protein · chain A against A, TM-score 0.81
- 2RNF · X-ray crystal structure of human ribonuclease 4 in complex with D(UP) · an experimental structure of the same protein · chain A against A, TM-score 0.81
- 2RNF · X-ray crystal structure of human ribonuclease 4 in complex with D(UP) · an experimental structure of the same protein · chain A against A, TM-score 0.81
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 P34096
- Elsewhere: UniProt P34096 · AlphaFold DB P34096
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