Research workbench
AlphaFold monomer V2.0 prediction for 4-hydroxyproline 2-epimerase (B9JQV3)
Analyse AlphaFold monomer V2.0 prediction for 4-hydroxyproline 2-epimerase (B9JQV3) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- B9JQV3
- Type
- protein
- Length
- 347 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x46EfCa788d03A3e879DAcDb96552AB8Bbc7e20b3
- UniProt
- B9JQV3
Structure
1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 347 | — | B9JQV3 |
Compared structures
- 4LB0 · Crystal structure of a hydroxyproline epimerase from agrobacterium vitis, target… · an experimental structure of the same protein · chain A against B, TM-score 0.98
- 4LB0 · Crystal structure of a hydroxyproline epimerase from agrobacterium vitis, target… · an experimental structure of the same protein · chain A against B, TM-score 0.98
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 B9JQV3
- Elsewhere: UniProt B9JQV3 · AlphaFold DB B9JQV3
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