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KINESIN 6

Analyse KINESIN 6 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5X3E
Type: protein
Length: 733 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Kinesin-like protein
UniProt: G5EG83
Ligands: SO4, IOD
Pockets: 9 · best druggability 0.66

Structure

x-ray diffraction · 2 distinct chains · 32% helix, 27% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Kinesin-like protein	protein	375	32% helix, 27% strand	G5EG83
B	Kinesin-like protein	protein	358	32% helix, 27% strand	G5EG83

Ligands and binding sites

SO4 · Sulfate ion · ion · 38 copies · chains A, B
IOD · Iodide ion · ion · 7 copies · chains A, B

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

Pockets

9 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	260	0.66	0.83	39	SO4, IOD
2	255	0.65	0.82	38	SO4, IOD
3	142	0.48	0.78	22	SO4
4	63	0.43	0.82	25	IOD
5	77	0.39	0.78	17	IOD

Interfaces

1 interface between chains.

A–B · 64 Å² buried · 0 hydrogen bonds · protein-protein

Compared structures

5X3E · kinesin 6 · the same entry in another collection · chain A against A, TM-score 1.00

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 G5EG83
Elsewhere: RCSB PDB 5X3E · PDBe 5X3E · UniProt G5EG83

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