MolNFT v1 · #5409 · protein
Structure of the second EPS15 homology domain of human EPS15, NMR, 20 structures
1EH2: “Structure of the second EPS15 homology domain of human EPS15, NMR, 20 structures”. Solution nmr. MolNFT v1 #5409 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1EH2
- Type
- protein
- Length
- 95 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P42566
Structure
solution nmr · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 95 | — | P42566 |
Compared structures
- 1EH2 · Structure of the second EPS15 homology domain of human EPS15, NMR, 20 structures · the same entry in another collection · chain A against A, TM-score 1.00
- P42566 · AlphaFold monomer V2.0 prediction for epidermal growth factor receptor substrate 15… · a predicted model of the same protein · chain A against A, TM-score 0.90
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 P42566
- Elsewhere: RCSB PDB 1EH2 · PDBe 1EH2 · UniProt P42566
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