Research workbench
The crystal structure of apo-HsMGME1 with Mn2+
Analyse The crystal structure of apo-HsMGME1 with Mn2+ in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5ZYW
- Type
- protein
- Length
- 233 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.2
- Source
- Homo sapiens
- Molecule
- Mitochondrial genome maintenance exonuclease 1
- EC
- 3.1.-.-
- UniProt
- Q9BQP7
- Ligands
- MN
- Pockets
- 1 · best druggability 0.70
Structure
x-ray diffraction · resolution 2.2 · 1 distinct chain · 41% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Mitochondrial genome maintenance exonuclease 1 (EC 3.1.-.-) | protein | 233 | 41% helix, 21% strand | Q9BQP7 |
Ligands and binding sites
- MN · Manganese (II) ion · metal · 3 copies · chains A
- TLA · L(+)-tartaric acid · additive · chains A
- GOL · Glycerol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 256 | 0.70 | 0.86 | 35 | TLA |
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 Q9BQP7
- Elsewhere: RCSB PDB 5ZYW · PDBe 5ZYW · UniProt Q9BQP7
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