MolNFT v1 · #179686 · protein
Structure of the C-terminal domain of the menangle virus phosphoprotein (residues 329 -388), fused to mbp. space group P21.
7KD4 · Maltodextrin-binding protein and phosphoprotein fusion…: “Structure of the C-terminal domain of the menangle virus phosphoprotein (residues 329 -388), fused to mbp.…”. X-ray diffraction, 2 ligands (GLC, SO4), 12 pockets (best…
- PDB
- 7KD4
- Type
- protein
- Length
- 862 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Maltodextrin-binding protein and phosphoprotein fusion protein
- UniProt
- A0A4P1LXE0, Q91MK1
- Ligands
- GLC, SO4
- Pockets
- 12 · best druggability 0.79
Structure
x-ray diffraction · 1 distinct chain · 50% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Maltodextrin-binding protein and phosphoprotein fusion protein | protein | 431 | 50% helix, 18% strand | A0A4P1LXE0, Q91MK1 |
Ligands and binding sites
- GLC · alpha-D-glucopyranose · sugar · 4 copies · chains A, B
- SO4 · Sulfate ion · ion · 16 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
12 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1061 | 0.79 | 0.81 | 85 | SO4 |
| 2 | 270 | 0.70 | 0.85 | 30 | GLC |
| 3 | 349 | 0.69 | 0.82 | 34 | GLC, SO4 |
| 4 | 242 | 0.50 | 0.75 | 42 | empty |
| 5 | 111 | 0.43 | 0.77 | 27 | empty |
Interfaces
1 interface between chains.
- A–B · 506 Ų buried · 9 hydrogen bonds · protein-protein
Compared structures
- 7KD4 · Structure of the C-terminal domain of the Menangle virus phosphoprotein (residues 329… · 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 A0A4P1LXE0
- Every structure of UniProt Q91MK1
- Elsewhere: RCSB PDB 7KD4 · PDBe 7KD4 · UniProt A0A4P1LXE0 · UniProt Q91MK1
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