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Human ubiquitous kinesin motor domain

Analyse Human ubiquitous kinesin motor domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1BG2
Type: protein
Length: 323 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Kinesin
UniProt: P33176
Ligands: ADP, MG
Pockets: 5 · best druggability 0.51

Structure

x-ray diffraction · 1 distinct chain · 32% helix, 28% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Kinesin	protein	323	32% helix, 28% strand	P33176

Ligands and binding sites

ADP · Adenosine-5'-diphosphate · ligand · chains A
MG · Magnesium ion · metal · chains A
ACT · Acetate ion · additive · 3 copies · 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	140	0.51	0.80	33	MG, ACT
2	100	0.49	0.81	20	empty
3	169	0.48	0.77	30	empty
4	59	0.30	0.76	16	empty
5	65	0.27	0.73	19	empty

Compared structures

1BG2 · Human ubiquitous kinesin motor domain · the same entry in another collection · chain A against A, TM-score 1.00
P33176 · AlphaFold monomer V2.0 prediction for kinesin-1 heavy chain (P33176) · a predicted model of the same protein · chain A against A, TM-score 0.93

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 P33176
Elsewhere: RCSB PDB 1BG2 · PDBe 1BG2 · UniProt P33176

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