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AlphaFold monomer V2.0 prediction for brisc complex subunit FAM175B (E2AB17)

Analyse AlphaFold monomer V2.0 prediction for brisc complex subunit FAM175B (E2AB17) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

Accession: E2AB17
Type: protein
Length: 471 residues
Chains: 1
Collection: MolNFT v1 / AlphaFold
Contract: 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner: 0x9F605311B7e26e76340423EfAfbE5e2EFc7A0b7C
UniProt: E2AB17

Structure

1 distinct chain.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	—	protein	471	—	E2AB17

Compared structures

5CW3 · Structure of CFBRCC36-CFKIAA0157 complex (zn edge) · an experimental structure of the same protein · chain A against B, TM-score 0.52
5CW3 · Structure of CfBRCC36-CfKIAA0157 complex (Zn Edge) · an experimental structure of the same protein · chain A against B, TM-score 0.52
5CW4 · Structure of CfBRCC36-CfKIAA0157 complex (Selenium Edge) · an experimental structure of the same protein · chain A against B, TM-score 0.51
5CW4 · Structure of CFBRCC36-CFKIAA0157 complex (selenium edge) · an experimental structure of the same protein · chain A against B, TM-score 0.51
5CW5 · Structure of CFBRCC36-CFKIAA0157 complex (qsq mutant) · an experimental structure of the same protein · chain A against D, TM-score 0.50
5CW5 · Structure of CfBRCC36-CfKIAA0157 complex (QSQ mutant) · an experimental structure of the same protein · chain A against D, TM-score 0.50

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 E2AB17
Elsewhere: UniProt E2AB17 · AlphaFold DB E2AB17

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