Research workbench

AlphaFold monomer V2.0 prediction for chaperone protein faee (P25401)

Analyse AlphaFold monomer V2.0 prediction for chaperone protein faee (P25401) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

Accession: P25401
Type: protein
Length: 258 residues
Chains: 1
Collection: MolNFT v1 / AlphaFold
Contract: 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner: 0xA2ED127c7DF83E1D9Fa8D7c517410A1D4A5B70F5
UniProt: P25401

Structure

1 distinct chain.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	—	protein	258	—	P25401

Compared structures

3GFU · FaeE-FaeG chaperone-major pilin complex of F4 ac 5/95 fimbriae · an experimental structure of the same protein · chain A against A, TM-score 0.82
3GFU · Faee-faeg chaperone-major pilin complex of F4 ac 5/95 fimbriae · an experimental structure of the same protein · chain A against A, TM-score 0.82
3GEW · FaeE-FaeG chaperone-major pilin complex of F4 ad fimbriae · an experimental structure of the same protein · chain A against C, TM-score 0.80
3GEW · Faee-faeg chaperone-major pilin complex of F4 ad fimbriae · an experimental structure of the same protein · chain A against C, TM-score 0.80
3F65 · The F4 fimbrial chaperone faee does not self-cap its interactive surfaces · an experimental structure of the same protein · chain A against A, TM-score 0.77
3F65 · The F4 fimbrial chaperone FaeE does not self-cap its interactive surfaces · an experimental structure of the same protein · chain A against A, TM-score 0.77

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 P25401
Elsewhere: UniProt P25401 · AlphaFold DB P25401

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