Research workbench
AlphaFold monomer V2.0 prediction for carboxypeptidase B (P15086)
Analyse AlphaFold monomer V2.0 prediction for carboxypeptidase B (P15086) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P15086
- Type
- protein
- Length
- 417 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xF8cD1d8d93E9783063700De244A6e3cf6A195579
- UniProt
- P15086
Structure
1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 417 | — | P15086 |
Compared structures
- 1KWM · Human procarboxypeptidase B: Three-dimensional structure and implications for… · an experimental structure of the same protein · chain A against A, TM-score 0.96
- 1KWM · Human procarboxypeptidase B: three-dimensional structure and implications for… · an experimental structure of the same protein · chain A against A, TM-score 0.96
- 1ZLI · Crystal structure of the tick carboxypeptidase inhibitor in complex with human… · an experimental structure of the same protein · chain A against A, TM-score 0.73
- 1ZLI · Crystal structure of the tick carboxypeptidase inhibitor in complex with human… · an experimental structure of the same protein · chain A against A, TM-score 0.73
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 P15086
- Elsewhere: UniProt P15086 · AlphaFold DB P15086
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