Research workbench
The solution NMR structure and dynamics of a recombinant onconase with altered N-terminal and MET23 residues
Analyse The solution NMR structure and dynamics of a recombinant onconase with altered… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1PU3
- Type
- protein
- Length
- 105 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- P-30 protein
- EC
- 3.1.27.-
- UniProt
- P22069
Structure
solution nmr · 1 distinct chain · 19% helix, 40% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | P-30 protein (EC 3.1.27.-) | protein | 105 | 19% helix, 40% strand | P22069 |
Modifications
Observed in the structure: 4 disulfide (disulfide).
Compared structures
- 1PU3 · The Solution NMR Structure and Dynamics of a Recombinant Onconase with Altered N-terminal… · the same entry in another collection · chain A against A, TM-score 1.00
- P22069 · AlphaFold monomer V2.0 prediction for protein P-30 (P22069) · a predicted model of the same protein · chain A against A, TM-score 0.96
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 P22069
- Elsewhere: RCSB PDB 1PU3 · PDBe 1PU3 · UniProt P22069
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