Research workbench
Crystal structure of an ehd ATPase involved in membrane remodelling
Analyse Crystal structure of an ehd ATPase involved in membrane remodelling in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2QPT
- Type
- protein
- Length
- 476 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Eh domain-containing protein-2
- UniProt
- Q8BH64
- Ligands
- ANP, MG, CA
- Pockets
- 5 · best druggability 0.76
Structure
x-ray diffraction · 1 distinct chain · 51% helix, 9% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Eh domain-containing protein-2 | protein | 476 | 51% helix, 9% strand | Q8BH64 |
Ligands and binding sites
- ANP · Phosphoaminophosphonic acid-adenylate ester · ligand · chains A
- MG · Magnesium ion · metal · chains A
- CA · Calcium ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 692 | 0.76 | 0.81 | 66 | empty |
| 2 | 130 | 0.59 | 0.85 | 29 | MG, ANP |
| 3 | 178 | 0.46 | 0.75 | 22 | empty |
| 4 | 123 | 0.38 | 0.74 | 22 | empty |
| 5 | 87 | 0.37 | 0.76 | 14 | empty |
Compared structures
- 2QPT · Crystal structure of an EHD ATPase involved in membrane remodelling · the same entry in another collection · chain A against A, TM-score 1.00
- Q8BH64 · AlphaFold monomer V2.0 prediction for eh domain-containing protein 2 (Q8BH64) · a predicted model of the same protein · chain A against A, TM-score 0.98
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 Q8BH64
- Elsewhere: RCSB PDB 2QPT · PDBe 2QPT · UniProt Q8BH64
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