Research workbench
Structure of the C-terminal domain of the menangle virus phosphoprotein (residues 329 -388), fused to mbp. space group P212121
Analyse Structure of the C-terminal domain of the menangle virus phosphoprotein… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7KD5
- Type
- protein
- Length
- 428 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Maltodextrin-binding protein and phosphoprotein fusion protein
- UniProt
- A0A4P1LXE0, Q91MK1
- Ligands
- PIN, PRO, GLC
- Pockets
- 3 · best druggability 0.68
Structure
x-ray diffraction · 1 distinct chain · 48% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Maltodextrin-binding protein and phosphoprotein fusion protein | protein | 428 | 48% helix, 18% strand | A0A4P1LXE0, Q91MK1 |
Ligands and binding sites
- PIN · Piperazine-N,N'-bis(2-ethanesulfonic acid) · ligand · 3 copies · chains A
- PRO · Proline · ligand · chains A
- GLC · alpha-D-glucopyranose · sugar · 2 copies · chains A
- EDO · 1,2-ethanediol · additive · 4 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 299 | 0.68 | 0.83 | 33 | GLC |
| 2 | 440 | 0.58 | 0.74 | 49 | EDO |
| 3 | 199 | 0.49 | 0.76 | 29 | empty |
Compared structures
- 7KD5 · 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 7KD5 · PDBe 7KD5 · UniProt A0A4P1LXE0 · UniProt Q91MK1
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