Research workbench

AlphaFold monomer V2.0 prediction for zinc finger protein 423 (Q2M1K9)

Analyse AlphaFold monomer V2.0 prediction for zinc finger protein 423 (Q2M1K9) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

Accession: Q2M1K9
Type: protein
Length: 1,284 residues
Chains: 1
Collection: MolNFT v1 / AlphaFold
Contract: 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner: 0x1054D383f4695fc7A5ecBD5BcA9BBC5F2f88B6c0
Molecule: Zinc finger protein 423
UniProt: Q2M1K9
Pockets: 8 · best druggability 0.75

Structure

1 distinct chain · 29% helix, 10% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Zinc finger protein 423	protein	1284	29% helix, 10% strand	Q2M1K9

Pockets

8 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1040	0.75	0.77	63	empty
2	227	0.64	0.83	26	empty
3	299	0.52	0.74	25	empty
4	236	0.52	0.76	25	empty
5	90	0.45	0.79	14	empty

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

2MDG · Solution NMR Structure of Zinc finger protein 423 from Homo sapiens, Northeast Structural… · an experimental structure of the same protein · chain A against A, TM-score 0.03
2MDG · Solution NMR structure of zinc finger protein 423 from homo sapiens, northeast structural… · an experimental structure of the same protein · chain A against A, TM-score 0.03

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 Q2M1K9
Elsewhere: UniProt Q2M1K9 · AlphaFold DB Q2M1K9

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