Research workbench
Crystal structure of the wd-repeat domain of human KIF21A
Analyse Crystal structure of the wd-repeat domain of human KIF21A in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7KLJ
- Type
- protein
- Length
- 639 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Isoform 2 of kinesin-like protein KIF21A
- UniProt
- Q7Z4S6
- Ligands
- UNX
- Pockets
- 3 · best druggability 0.83
Structure
x-ray diffraction · 2 distinct chains · 0% helix, 54% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Isoform 2 of kinesin-like protein KIF21A | protein | 324 | 0% helix, 54% strand | Q7Z4S6 |
| B | Isoform 2 of kinesin-like protein KIF21A | protein | 315 | 0% helix, 55% strand | Q7Z4S6 |
Ligands and binding sites
- UNX · Unknown atom or ion · ion · 5 copies · chains A, B
- EDO · 1,2-ethanediol · additive · 2 copies · chains A, B
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 | 1173 | 0.83 | 0.84 | 94 | UNX |
| 2 | 714 | 0.74 | 0.79 | 57 | UNX |
| 3 | 81 | 0.38 | 0.77 | 19 | empty |
Interfaces
1 interface between chains.
- A–B · 586 Ų buried · 5 hydrogen bonds · protein-protein
Compared structures
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 Q7Z4S6
- Elsewhere: RCSB PDB 7KLJ · PDBe 7KLJ · UniProt Q7Z4S6
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