Research workbench
A novel binding mode of maguk gk domain revealed by dlg gk domain in complex with KIF13B mbs domain
Analyse A novel binding mode of maguk gk domain revealed by dlg gk domain in complex… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5B64
- Type
- protein
- Length
- 296 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Dlg gk; Protein KIF13B
- UniProt
- E9Q4K7
- Ligands
- SO4
- Pockets
- 1 · best druggability 0.74
Structure
x-ray diffraction · 2 distinct chains · 47% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Dlg gk | protein | 180 | 44% helix, 21% strand | — |
| B | Protein KIF13B | protein | 116 | 52% helix, 18% strand | E9Q4K7 |
Ligands and binding sites
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 | 910 | 0.74 | 0.78 | 77 | SO4 |
Interfaces
1 interface between chains.
- A–B · 892 Ų buried · 14 hydrogen bonds · protein-protein
Compared structures
- 5B64 · A novel binding mode of MAGUK GK domain revealed by DLG GK domain in complex with KIF13B… · 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 E9Q4K7
- Elsewhere: RCSB PDB 5B64 · PDBe 5B64 · UniProt E9Q4K7
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