Research workbench
The cryo-EM MAP of KIF18A bound to kifbp
Analyse The cryo-EM MAP of KIF18A bound to kifbp in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7RSI
- Type
- protein
- Length
- 686 residues
- Chains
- 2
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Kif-binding protein; Kinesin-like protein KIF18A
- UniProt
- Q96EK5, Q8NI77
- Ligands
- ADP, MG
- Pockets
- 15 · best druggability 0.72
Structure
electron microscopy · 2 distinct chains · 56% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B | Kif-binding protein | protein | 392 | 74% helix, 0% strand | Q96EK5 |
| C | Kinesin-like protein KIF18A | protein | 294 | 30% helix, 29% strand | Q8NI77 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
15 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 137 | 0.72 | 0.91 | 27 | empty |
| 2 | 288 | 0.72 | 0.85 | 45 | empty |
| 3 | 54 | 0.70 | 0.97 | 19 | empty |
| 4 | 486 | 0.70 | 0.80 | 71 | empty |
| 5 | 96 | 0.68 | 0.91 | 22 | empty |
Interfaces
1 interface between chains.
- B–C · 1082 Ų buried · 18 hydrogen bonds · protein-protein
Compared structures
- 7RSI · The cryo-EM map of KIF18A bound to KIFBP · the same entry in another collection · chain B against B, TM-score 1.00
- Q8NI77 · AlphaFold monomer V2.0 prediction for kinesin-like protein KIF18A (Q8NI77) · a predicted model of the same protein · chain C against A, TM-score 0.88
- Q96EK5 · AlphaFold monomer V2.0 prediction for kif-binding protein (Q96EK5) · a predicted model of the same protein · chain B against A, TM-score 0.85
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 Q96EK5
- Every structure of UniProt Q8NI77
- Elsewhere: RCSB PDB 7RSI · PDBe 7RSI · UniProt Q96EK5 · UniProt Q8NI77
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