Research workbench
Structure of the second EPS15 homology domain of human EPS15, NMR, 20 structures
Analyse Structure of the second EPS15 homology domain of human EPS15, NMR, 20 structures in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- 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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