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Crystal structure of human kinesin EG5 in complex with 3-(((2-AMINOETHYL)SULFANYL)(3-ethylphenyl) PHENYLMETHYL)PHENOL

Analyse Crystal structure of human kinesin EG5 in complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4BBG
Type: protein
Length: 336 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Kinesin-like protein KIF11
UniProt: P52732
Ligands: ADP, V02, MG, CL
Pockets: 3 · best druggability 0.62

Structure

x-ray diffraction · 1 distinct chain · 32% helix, 31% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Kinesin-like protein KIF11	protein	336	32% helix, 31% strand	P52732

Ligands and binding sites

ADP · Adenosine-5'-diphosphate · ligand · chains A
V02 · 3-[(R)-2-azanylethylsulfanyl-(3-ethylphenyl)-phenyl-methyl]phenol · ligand · chains A
MG · Magnesium ion · metal · chains A
CL · Chloride ion · ion · 5 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, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	279	0.62	0.80	31	empty
2	177	0.61	0.83	25	V02
3	134	0.45	0.78	35	ADP, MG

Compared structures

4BBG · Crystal structure of human kinesin Eg5 in complex with… · 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 P52732
Elsewhere: RCSB PDB 4BBG · PDBe 4BBG · UniProt P52732

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