Research workbench

AlphaFold monomer V2.0 prediction for ephrin-A5 (P52803)

Analyse AlphaFold monomer V2.0 prediction for ephrin-A5 (P52803) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

Accession: P52803
Type: protein
Length: 228 residues
Chains: 1
Collection: MolNFT v1 / AlphaFold
Contract: 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner: 0x9188600a0FCa2914254C94299b1bd9721Bc4D500
UniProt: P52803

Structure

1 distinct chain.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	—	protein	228	—	P52803

Compared structures

4M4R · Epha4 ectodomain complex with ephrin a5 · an experimental structure of the same protein · chain A against B, TM-score 0.61
4M4R · EPHA4 ectodomain complex with ephrin A5 · an experimental structure of the same protein · chain A against B, TM-score 0.61
4L0P · Structure of the human EPHA3 receptor ligand binding domain complexed with ephrin-A5 · an experimental structure of the same protein · chain A against B, TM-score 0.60
4L0P · Structure of the human EphA3 receptor ligand binding domain complexed with ephrin-A5 · an experimental structure of the same protein · chain A against B, TM-score 0.60
2X11 · Crystal structure of the complete EPHA2 ectodomain in complex with ephrin A5 receptor… · an experimental structure of the same protein · chain A against B, TM-score 0.59
2X11 · Crystal structure of the complete EphA2 ectodomain in complex with ephrin A5 receptor… · an experimental structure of the same protein · chain A against B, TM-score 0.59

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 P52803
Elsewhere: UniProt P52803 · AlphaFold DB P52803

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