Research workbench
AlphaFold monomer V2.0 prediction for antileukoproteinase (P03973)
Analyse AlphaFold monomer V2.0 prediction for antileukoproteinase (P03973) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P03973
- Type
- protein
- Length
- 132 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x9F605311B7e26e76340423EfAfbE5e2EFc7A0b7C
- Molecule
- Antileukoproteinase
- UniProt
- P03973
Structure
1 distinct chain · 5% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Antileukoproteinase | protein | 132 | 5% helix, 17% strand | P03973 |
Modifications
Observed in the structure: 8 disulfide (disulfide).
Compared structures
- 2Z7F · Crystal structure of the complex of human neutrophil elastase with 1/2SLPI · an experimental structure of the same protein · chain A against I, TM-score 0.37
- 2Z7F · Crystal structure of the complex of human neutrophil elastase with 1/2SLPI · an experimental structure of the same protein · chain A against I, TM-score 0.37
- 4DOQ · Crystal structure of the complex of porcine pancreatic trypsin with 1/2SLPI · an experimental structure of the same protein · chain A against B, TM-score 0.35
- 4DOQ · Crystal structure of the complex of Porcine Pancreatic Trypsin with 1/2SLPI · an experimental structure of the same protein · chain A against B, TM-score 0.35
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 P03973
- Elsewhere: UniProt P03973 · AlphaFold DB P03973
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