MolNFT v1 · #111937 · protein
AlphaFold monomer V2.0 prediction for ephrin-A5 (P52803)
P52803: “AlphaFold monomer V2.0 prediction for ephrin-A5 (P52803)”. MolNFT v1 #111937 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- 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
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.