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Motor domain of human kinesin family member C1

Analyse Motor domain of human kinesin family member C1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5WDH
Type: protein
Length: 296 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Kinesin-like protein KIFC1
UniProt: Q9BW19
Ligands: ADP, MG, UNX
Pockets: 3 · best druggability 0.45

Structure

x-ray diffraction · 1 distinct chain · 35% helix, 28% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Kinesin-like protein KIFC1	protein	296	35% helix, 28% strand	Q9BW19

Ligands and binding sites

ADP · Adenosine-5'-diphosphate · ligand · chains A
MG · Magnesium ion · metal · chains A
UNX · Unknown atom or ion · ion · 6 copies · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	91	0.45	0.80	18	empty
2	57	0.40	0.81	12	empty
3	95	0.36	0.75	22	MG

Compared structures

5WDH · Motor domain of human kinesin family member C1 · the same entry in another collection · chain A against A, TM-score 1.00
Q9BW19 · AlphaFold monomer V2.0 prediction for kinesin-like protein KIFC1 (Q9BW19) · a predicted model of the same protein · chain A against A, TM-score 0.99

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 Q9BW19
Elsewhere: RCSB PDB 5WDH · PDBe 5WDH · UniProt Q9BW19

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