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AlphaFold monomer V2.0 prediction for sal-like protein 4 (Q9UJQ4)

Analyse AlphaFold monomer V2.0 prediction for sal-like protein 4 (Q9UJQ4) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

Accession: Q9UJQ4
Type: protein
Length: 1,053 residues
Chains: 1
Collection: MolNFT v1 / AlphaFold
Contract: 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner: 0x7782F4817b37743d738e9aF842bf74bd50f2015E
Molecule: Sal-like protein 4
UniProt: Q9UJQ4
Pockets: 1 · best druggability 0.30

Structure

1 distinct chain · 18% helix, 3% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Sal-like protein 4	protein	1053	18% helix, 3% strand	Q9UJQ4

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	64	0.30	0.74	17	empty

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

7Y3M · Structure of SALL4 ZFC1 bound with 16 bp AT-rich dsDNA · an experimental structure of the same protein · chain A against C, TM-score 0.07
7Y3K · Structure of SALL4 ZFC4 bound with 16 bp AT-rich dsDNA · an experimental structure of the same protein · chain A against A, TM-score 0.05
7Y3I · Structure of DNA bound SALL4 · an experimental structure of the same protein · chain A against A, TM-score 0.05
8CUC · Crystal structure analysis of SALL4 zinc finger domain in complex with DNA · an experimental structure of the same protein · chain A against F, TM-score 0.05

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 Q9UJQ4
Elsewhere: UniProt Q9UJQ4 · AlphaFold DB Q9UJQ4

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