MolNFT v1 · #142261 · protein
The crystal structure of apo-HSMGME1 with MN2+
5ZYW · Mitochondrial genome maintenance exonuclease 1: “The crystal structure of apo-HSMGME1 with MN2+”. X-ray diffraction, 1 ligand (MN), 1 pocket (best druggability 0.70). MolNFT v1 #142261 on GenesisL1: 3D structure, binding sites and…
- PDB
- 5ZYW
- Type
- protein
- Length
- 233 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Mitochondrial genome maintenance exonuclease 1
- EC
- 3.1.-.-
- UniProt
- Q9BQP7
- Ligands
- MN
- Pockets
- 1 · best druggability 0.70
Structure
x-ray diffraction · 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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