MolNFT v1 · #6305 · protein
Structure of the second EPS15 homology domain of human EPS15 in complex with ptgssstnpfr
1F8H · Epidermal growth factor receptor substrate 15: “Structure of the second EPS15 homology domain of human EPS15 in complex with ptgssstnpfr”. Solution nmr, 1 ligand (CA). MolNFT v1 #6305 on GenesisL1: 3D structure, binding sites and…
- 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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