Research workbench
ATPase crystal structure
Analyse ATPase crystal structure in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4BYG
- Type
- protein
- Length
- 663 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Copper efflux ATPase
- EC
- 3.6.3.-
- UniProt
- Q5ZWR1
- Ligands
- ALF, MG, K
- Pockets
- 8 · best druggability 0.70
Structure
x-ray diffraction · 1 distinct chain · 48% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Copper efflux ATPase (EC 3.6.3.-) | protein | 663 | 48% helix, 14% strand | Q5ZWR1 |
Ligands and binding sites
- ALF · Tetrafluoroaluminate ion · ligand · chains A
- MG · Magnesium ion · metal · chains A
- K · Potassium ion · metal · chains A
- 15P · Polyethylene glycol (N=34) · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 611 | 0.70 | 0.79 | 69 | empty |
| 2 | 278 | 0.61 | 0.80 | 37 | empty |
| 3 | 134 | 0.42 | 0.76 | 24 | K |
| 4 | 66 | 0.37 | 0.78 | 18 | empty |
| 5 | 100 | 0.36 | 0.74 | 27 | empty |
Compared structures
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 Q5ZWR1
- Elsewhere: RCSB PDB 4BYG · PDBe 4BYG · UniProt Q5ZWR1
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