MolNFT v1 · #64629 · protein
1.2 ångström structure of the exonuclease III homologue MTH0212
3G91 · Exodeoxyribonuclease: “1.2 ångström structure of the exonuclease III homologue MTH0212”. X-ray diffraction, 2 ligands (MG, PO4), 1 pocket (best druggability 0.42). MolNFT v1 #64629 on GenesisL1: 3D structure, binding sites and…
- PDB
- 3G91
- Type
- protein
- Length
- 260 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Exodeoxyribonuclease
- EC
- 3.1.11.2
- UniProt
- O26314
- Ligands
- MG, PO4
- Pockets
- 1 · best druggability 0.42
Structure
x-ray diffraction · 1 distinct chain · 30% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Exodeoxyribonuclease (EC 3.1.11.2) | protein | 260 | 30% helix, 27% strand | O26314 |
Ligands and binding sites
- MG · Magnesium ion · metal · chains A
- PO4 · Phosphate ion · ion · chains A
- GOL · Glycerol · additive · chains A
- PEG · Di(hydroxyethyl)ether · additive · chains A
- PG4 · Tetraethylene glycol · 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, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 133 | 0.42 | 0.75 | 26 | PO4, MG |
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 O26314
- Elsewhere: RCSB PDB 3G91 · PDBe 3G91 · UniProt O26314
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