Research workbench

AlphaFold monomer V2.0 prediction for zwei ig domain protein zig-4 (G5ECB1)

Analyse AlphaFold monomer V2.0 prediction for zwei ig domain protein zig-4 (G5ECB1) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

Accession: G5ECB1
Type: protein
Length: 253 residues
Chains: 1
Collection: MolNFT v1 / AlphaFold
Contract: 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner: 0xbb2F1C7CB3A1eeFAc24fCa72cc627162D5413FD7
Molecule: Zwei ig domain protein zig-4
UniProt: G5ECB1
Pockets: 2 · best druggability 0.65

Structure

1 distinct chain · 19% helix, 44% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Zwei ig domain protein zig-4	protein	253	19% helix, 44% strand	G5ECB1

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	62	0.65	0.94	19	empty
2	53	0.28	0.74	12	empty

Modifications

Observed in the structure: 3 disulfide (disulfide).

Compared structures

8TKT · ZIG-4-INS-6 complex, C-centered monoclinic form · an experimental structure of the same protein · chain A against C, TM-score 0.81
8TKU · ZIG-4-INS-6 complex, primitive monoclinic form · an experimental structure of the same protein · chain A against A, TM-score 0.81
8TK9 · ZIG-4-INS-6 complex, tetragonal form · an experimental structure of the same protein · chain A against A, TM-score 0.79

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 G5ECB1
Elsewhere: UniProt G5ECB1 · AlphaFold DB G5ECB1

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