Research workbench
AlphaFold monomer V2.0 prediction for dnaj homolog subfamily C member 5 (Q9H3Z4)
Analyse AlphaFold monomer V2.0 prediction for dnaj homolog subfamily C member 5 (Q9H3Z4) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q9H3Z4
- Type
- protein
- Length
- 198 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xe31a910f6C16a75742b91e7617931F9bE87c1D6c
- UniProt
- Q9H3Z4
Structure
1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 198 | — | Q9H3Z4 |
Compared structures
- 2N05 · Solution Structure of the non-phosphorylated N-terminal region of Human Cysteine String… · an experimental structure of the same protein · chain A against A, TM-score 0.35
- 2N05 · Solution structure of the non-phosphorylated N-terminal region of human cysteine string… · an experimental structure of the same protein · chain A against A, TM-score 0.35
- 2N04 · Solution Structure of the phosphorylated N-terminal region of Human Cysteine String… · an experimental structure of the same protein · chain A against A, TM-score 0.32
- 2N04 · Solution structure of the phosphorylated N-terminal region of human cysteine string… · an experimental structure of the same protein · chain A against A, TM-score 0.32
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 Q9H3Z4
- Elsewhere: UniProt Q9H3Z4 · AlphaFold DB Q9H3Z4
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