Research workbench
AlphaFold monomer V2.0 prediction for proproteinase E (P05805)
Analyse AlphaFold monomer V2.0 prediction for proproteinase E (P05805) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P05805
- Type
- protein
- Length
- 253 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x91cB1A9982C8247E3BC25D698cCCD89D78d736B6
- UniProt
- P05805
Structure
1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 253 | — | P05805 |
Compared structures
- 1PYT · Ternary complex of procarboxypeptidase a, proproteinase E, and chymotrypsinogen C · an experimental structure of the same protein · chain A against C, TM-score 0.92
- 1PYT · Ternary complex of procarboxypeptidase a, proproteinase E, and chymotrypsinogen C · an experimental structure of the same protein · chain A against C, TM-score 0.92
- 1FON · Crystal structure of bovine procarboxypeptidase a-S6 subunit III, a highly structured… · an experimental structure of the same protein · chain A against B, TM-score 0.83
- 1FON · Crystal structure of bovine procarboxypeptidase a-S6 subunit III, a highly structured… · an experimental structure of the same protein · chain A against B, TM-score 0.83
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 P05805
- Elsewhere: UniProt P05805 · AlphaFold DB P05805
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