Research workbench
Structure of the second EPS15 homology domain of human EPS15 in complex with ptgssstnpfr
Analyse Structure of the second EPS15 homology domain of human EPS15 in complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1F8H
- Type
- protein
- Length
- 101 residues
- Chains
- 2
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Epidermal growth factor receptor substrate 15; Ptgssstnpfr
- UniProt
- P42566
- Ligands
- CA
Structure
solution nmr · 2 distinct chains · 48% helix, 2% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Epidermal growth factor receptor substrate 15 | protein | 95 | 51% helix, 2% strand | P42566 |
| B | Ptgssstnpfr | protein | 6 | 0% helix, 0% strand | — |
Ligands and binding sites
- CA · Calcium ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–B · 349 Ų buried · 4 hydrogen bonds · protein-protein
Compared structures
- 1F8H · Structure of the second EPS15 homology domain of human EPS15 in complex with ptgssstnpfr · 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 1F8H · PDBe 1F8H · UniProt P42566
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