Research workbench
Neisseria DNA mimic protein DMP12
Analyse Neisseria DNA mimic protein DMP12 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3W1O
- Type
- protein
- Length
- 230 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- DNA mimic protein DMP12
- UniProt
- Q9JXC6
- Ligands
- MG
- Pockets
- 1 · best druggability 0.57
Structure
x-ray diffraction · 1 distinct chain · 50% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | DNA mimic protein DMP12 | protein | 115 | 50% helix, 15% strand | Q9JXC6 |
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
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 | 69 | 0.57 | 0.89 | 18 | empty |
Interfaces
1 interface between chains.
- A–B · 926 Ų buried · 10 hydrogen bonds · protein-protein
Compared structures
- 3W1O · Neisseria DNA mimic protein DMP12 · the same entry in another collection · chain A against A, TM-score 1.00
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 Q9JXC6
- Elsewhere: RCSB PDB 3W1O · PDBe 3W1O · UniProt Q9JXC6
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