MolNFT v1 · #38946 · protein
Crystal structure of the KIF2C motor domain
2HEH · KIF2C protein: “Crystal structure of the KIF2C motor domain”. X-ray diffraction, 3 ligands (ADP, MG, UNX), 1 pocket (best druggability 0.47). MolNFT v1 #38946 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 2HEH
- Type
- protein
- Length
- 324 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- KIF2C protein
- UniProt
- Q99661
- Ligands
- ADP, MG, UNX
- Pockets
- 1 · best druggability 0.47
Structure
x-ray diffraction · 1 distinct chain · 37% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | KIF2C protein | protein | 324 | 37% helix, 29% strand | Q99661 |
Ligands and binding sites
- ADP · Adenosine-5'-diphosphate · ligand · chains A
- MG · Magnesium ion · metal · chains A
- UNX · Unknown atom or ion · ion · 10 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 124 | 0.47 | 0.78 | 21 | UNX |
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 Q99661
- Elsewhere: RCSB PDB 2HEH · PDBe 2HEH · UniProt Q99661
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