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3D solution structure of human angiogenin determined by 1H, 15N NMR spectroscopy, 30 structures
Analyse 3D solution structure of human angiogenin determined by 1H, 15N NMR… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1AWZ
- Type
- protein
- Length
- 123 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Angiogenin
- EC
- 3.1.27.-
- UniProt
- P03950
Structure
solution nmr · 1 distinct chain · 21% helix, 35% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Angiogenin (EC 3.1.27.-) | protein | 123 | 21% helix, 35% strand | P03950 |
Modifications
Observed in the structure: 3 disulfide (disulfide).
Compared structures
- 1AWZ · 3D solution structure of human angiogenin determined by 1H, 15N NMR spectroscopy, 30… · the same entry in another collection · chain A against A, TM-score 1.00
- P03950 · AlphaFold monomer V2.0 prediction for angiogenin (P03950) · a predicted model of the same protein · chain A against A, TM-score 0.94
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 P03950
- Elsewhere: RCSB PDB 1AWZ · PDBe 1AWZ · UniProt P03950
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