Research workbench

AlphaFold monomer V2.0 prediction for ephrin type-B receptor 1 (P54762)

Analyse AlphaFold monomer V2.0 prediction for ephrin type-B receptor 1 (P54762) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

Accession: P54762
Type: protein
Length: 984 residues
Chains: 1
Collection: MolNFT v1 / AlphaFold
Contract: 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner: 0x9188600a0FCa2914254C94299b1bd9721Bc4D500
UniProt: P54762

Structure

1 distinct chain.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	—	protein	984	—	P54762

Compared structures

5MJB · Kinase domain of human EphB1, G703C mutant, covalently bound to a quinazoline-based… · an experimental structure of the same protein · chain A against A, TM-score 0.27
5MJB · Kinase domain of human EPHB1, G703C mutant, covalently bound to a quinazoline-based… · an experimental structure of the same protein · chain A against A, TM-score 0.27
5MJA · Kinase domain of human EPHB1 bound to a quinazoline-based inhibitor · an experimental structure of the same protein · chain A against B, TM-score 0.27
5MJA · Kinase domain of human EphB1 bound to a quinazoline-based inhibitor · an experimental structure of the same protein · chain A against B, TM-score 0.27
3ZFX · Crystal structure of EPHB1 · an experimental structure of the same protein · chain A against A, TM-score 0.27
3ZFX · Crystal structure of EphB1 · an experimental structure of the same protein · chain A against A, TM-score 0.27

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 P54762
Elsewhere: UniProt P54762 · AlphaFold DB P54762

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