Research workbench
EG5-3
Analyse EG5-3 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4B7B
- Type
- protein
- Length
- 329 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Kinesin-like protein KIF11
- UniProt
- P52732
- Ligands
- ADP, CD, CO, CA, CL
- Pockets
- 4 · best druggability 0.50
Structure
x-ray diffraction · 1 distinct chain · 34% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Kinesin-like protein KIF11 | protein | 329 | 34% helix, 30% strand | P52732 |
Ligands and binding sites
- ADP · Adenosine-5'-diphosphate · ligand · chains A
- CD · Cadmium ion · metal · 11 copies · chains A
- CO · Cobalt (II) ion · metal · 5 copies · chains A
- CA · Calcium ion · metal · chains A
- CL · Chloride ion · ion · 10 copies · chains A
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 | 155 | 0.50 | 0.78 | 23 | empty |
| 2 | 59 | 0.32 | 0.77 | 20 | CD |
| 3 | 50 | 0.28 | 0.75 | 11 | empty |
| 4 | 51 | 0.27 | 0.75 | 15 | empty |
Compared structures
- 4B7B · Eg5-3 · 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 P52732
- Elsewhere: RCSB PDB 4B7B · PDBe 4B7B · UniProt P52732
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