MolNFT v1 · #174827 · protein
AlphaFold monomer V2.0 prediction for segmentation polarity homeobox protein engrailed (P02836)
P02836: “AlphaFold monomer V2.0 prediction for segmentation polarity homeobox protein engrailed (P02836)”. MolNFT v1 #174827 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- Accession
- P02836
- Type
- protein
- Length
- 552 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x8A081A73273877f549f82C9b9Ec83bc99bc11351
- UniProt
- P02836
Structure
1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 552 | — | P02836 |
Compared structures
- 6M3D · X-ray crystal structure of tandemly connected engrailed homeodomains (EHD) with R53A… · an experimental structure of the same protein · chain A against C, TM-score 0.11
- 6M3D · X-ray crystal structure of tandemly connected engrailed homeodomains (ehd) with R53A… · an experimental structure of the same protein · chain A against C, TM-score 0.11
- 1HDD · Crystal structure of an engrailed homeodomain-DNA complex at 2.8 ångströms resolution: a… · an experimental structure of the same protein · chain A against C, TM-score 0.10
- 1HDD · Crystal structure of an engrailed homeodomain-DNA complex at 2.8 ångströms resolution: a… · an experimental structure of the same protein · chain A against C, TM-score 0.10
- 2HOS · Phage-Selected Homeodomain Bound to Unmodified DNA · an experimental structure of the same protein · chain A against B, TM-score 0.10
- 2HOS · Phage-selected homeodomain bound to unmodified DNA · an experimental structure of the same protein · chain A against B, TM-score 0.10
- 2HOT · Phage selected homeodomain bound to modified DNA · an experimental structure of the same protein · chain A against B, TM-score 0.10
- 2HOT · Phage selected homeodomain bound to modified DNA · an experimental structure of the same protein · chain A against B, TM-score 0.10
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 P02836
- Elsewhere: UniProt P02836 · AlphaFold DB P02836
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