MolNFT v2 · #143684 · protein
Proton pyrophosphatase-E225H mutant
6AFZ: “Proton pyrophosphatase-E225H mutant”. X-ray diffraction at 2.483, 4 ligands (1PG, MG, K). MolNFT v2 #143684 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6AFZ
- Type
- protein
- Length
- 1,480 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.483
- Source
- Vigna radiata var. radiata
- UniProt
- P21616
- Ligands
- 1PG, MG, K, PO4
Structure
x-ray diffraction · resolution 2.483 · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | — | protein | 740 | — | P21616 |
Ligands and binding sites
- 1PG · 2-(2-{2-[2-(2-methoxy-ethoxy)-ethoxy]-ethoxy}-ethoxy)-ethanol · ligand · 7 copies · chains A, B
- MG · Magnesium ion · metal · 10 copies · chains A, B
- K · Potassium ion · metal · 2 copies · chains A, B
- PO4 · Phosphate ion · ion · 4 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
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 P21616
- Elsewhere: RCSB PDB 6AFZ · PDBe 6AFZ · UniProt P21616
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