Research workbench
Crystal structure of the KIF4 motor domain complexed with mg-amppnp
Analyse Crystal structure of the KIF4 motor domain complexed with mg-amppnp in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3ZFD
- Type
- protein
- Length
- 340 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Chromosome-associated kinesin KIF4
- EC
- 3.6.4.4
- UniProt
- P33174
- Ligands
- ANP, MG
- Pockets
- 5 · best druggability 0.56
Structure
x-ray diffraction · 1 distinct chain · 33% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Chromosome-associated kinesin KIF4 (EC 3.6.4.4) | protein | 340 | 33% helix, 31% strand | P33174 |
Ligands and binding sites
- ANP · Phosphoaminophosphonic acid-adenylate ester · ligand · chains A
- MG · Magnesium ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 272 | 0.56 | 0.77 | 37 | empty |
| 2 | 190 | 0.53 | 0.78 | 49 | MG, ANP |
| 3 | 54 | 0.44 | 0.84 | 16 | empty |
| 4 | 100 | 0.43 | 0.78 | 17 | empty |
| 5 | 69 | 0.33 | 0.75 | 17 | empty |
Compared structures
- 3ZFD · Crystal Structure of the Kif4 Motor Domain Complexed With Mg-AMPPNP · the same entry in another collection · chain A against A, TM-score 1.00
- P33174 · AlphaFold monomer V2.0 prediction for chromosome-associated kinesin KIF4 (P33174) · a predicted model of the same protein · chain A against A, TM-score 0.94
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 P33174
- Elsewhere: RCSB PDB 3ZFD · PDBe 3ZFD · UniProt P33174
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