Research workbench
MTH0212 (wt) crystallized in a monoclinic space group
Analyse MTH0212 (wt) crystallized in a monoclinic space group in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3G1K
- Type
- protein
- Length
- 512 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Exodeoxyribonuclease
- EC
- 3.1.11.2
- UniProt
- O26314
- Ligands
- MG
- Pockets
- 4 · best druggability 0.80
Structure
x-ray diffraction · 1 distinct chain · 29% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Exodeoxyribonuclease (EC 3.1.11.2) | protein | 256 | 29% helix, 27% strand | O26314 |
Ligands and binding sites
- MG · Magnesium ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 813 | 0.80 | 0.83 | 74 | MG |
| 2 | 202 | 0.50 | 0.76 | 27 | empty |
| 3 | 157 | 0.48 | 0.77 | 26 | MG |
| 4 | 52 | 0.28 | 0.74 | 12 | empty |
Interfaces
1 interface between chains.
- A–B · 641 Ų buried · 6 hydrogen bonds · protein-protein
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 3G1K · PDBe 3G1K · UniProt O26314
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