Research workbench
AlphaFold monomer V2.0 prediction for intracellular endo- alpha-(1->5)-L-arabinanase (Q93HT9)
Analyse AlphaFold monomer V2.0 prediction for intracellular endo… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q93HT9
- Type
- protein
- Length
- 313 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xb3c0C983Fc44934AC589D7131C08a72544EBB92E
- UniProt
- Q93HT9
Structure
1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 313 | — | Q93HT9 |
Compared structures
- 6A8H · Crystal structure of endo-arabinanase abn-ts D27A mutant in complex with arabinotriose · an experimental structure of the same protein · chain A against A, TM-score 0.99
- 6A8H · Crystal structure of endo-arabinanase ABN-TS D27A mutant in complex with arabinotriose · an experimental structure of the same protein · chain A against A, TM-score 0.99
- 6A8I · Crystal structure of endo-arabinanase ABN-TS D147N mutant in complex with arabinohexaose · an experimental structure of the same protein · chain A against B, TM-score 0.99
- 6A8I · Crystal structure of endo-arabinanase abn-ts D147N mutant in complex with arabinohexaose · an experimental structure of the same protein · chain A against A, TM-score 0.99
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 Q93HT9
- Elsewhere: UniProt Q93HT9 · AlphaFold DB Q93HT9
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