3HQD: Human kinesin Eg5 motor domain

Human kinesin Eg5 motor domain in complex with AMPPNP and Mg2+. Determined by X-ray diffraction at 2.19 Å resolution. Released 8 Dec 2009.

Method: X-ray diffraction
Resolution: 2.19 Å
Organism: Homo sapiens
Chains: 2
Atoms: 5,832
Mol. weight: 83.49 kDa
Ligands: PO4, MG, ANP
Released: 8 Dec 2009

Explore 3HQD in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3HQD contains 35 α-helices and 46 β-strands across 2 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 17 helices, 23 β-strands

Element	Residues	Length	Sheet
β-strand	18	1	1
α-helix	19	1
β-strand	20-25	6	2
α-helix	26-28	3
α-helix	30-34	5
β-strand	39	1	3
β-strand	41-44	4	4
β-strand	49-53	5	4
β-strand	63-67	5	4
β-strand	70-72	3	2
α-helix	78-81	4
α-helix	82-86	5
α-helix	87-94	8
β-strand	98-104	7	2
α-helix	111-115	5
β-strand	117	1	5
α-helix	121-123	3
β-strand	133	1	5
α-helix	135-150	16
β-strand	153-164	12	2
β-strand	167-170	4	2
α-helix	178-181	4
β-strand	182	1	2
β-strand	183-187	5	6
β-strand	190-197	8	6
β-strand	202-204	3	2
α-helix	207-220	14
β-strand	223-224	2	7
β-strand	232-233	2	7
β-strand	236-248	13	2
β-strand	254-265	12	2
α-helix	272-275	4
α-helix	279-303	25
α-helix	311-313	3
α-helix	315-319	5
β-strand	328-336	9	2
β-strand	339	1	3
α-helix	340-342	3
α-helix	343-357	15
β-strand	360	1	1

Chain B: 18 helices, 23 β-strands

Element	Residues	Length	Sheet
β-strand	18	1	8
α-helix	19	1
β-strand	20-25	6	9
α-helix	26-28	3
α-helix	30-34	5
α-helix	37-38	2
β-strand	39	1	10
β-strand	41-44	4	11
β-strand	49-53	5	11
β-strand	63-67	5	11
β-strand	70-72	3	9
α-helix	78-81	4
α-helix	82-86	5
α-helix	87-94	8
β-strand	98-104	7	9
α-helix	111-115	5
β-strand	117	1	12
α-helix	127-129	3
β-strand	133	1	12
α-helix	135-150	16
β-strand	153-163	11	9
β-strand	168-170	3	9
β-strand	182	1	9
β-strand	183-186	4	13
β-strand	194-197	4	13
β-strand	202-204	3	9
α-helix	207-220	14
β-strand	223-224	2	14
β-strand	232-233	2	14
β-strand	236-248	13	9
β-strand	254-265	12	9
α-helix	272-275	4
α-helix	280-303	24
α-helix	311-313	3
α-helix	315-320	6
α-helix	321-323	3
β-strand	329-336	8	9
β-strand	339	1	10
α-helix	340-342	3
α-helix	343-356	14
β-strand	360	1	8

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Kinesin-like protein KIF11	A, B	protein	369	Homo sapiens	P52732 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>3HQD_1 Kinesin-like protein KIF11 (chains A, B)
MASQPNSSAKKKEEKGKNIQVVVRCRPFNLAERKASAHSIVECDPVRKEVSVRTGGLADK
SSRKTYTFDMVFGASTKQIDVYRSVVCPILDEVIMGYNCTIFAYGQTGTGKTFTMEGERS
PNEEYTWEEDPLAGIIPRTLHQIFEKLTDNGTEFSVKVSLLEIYNEELFDLLNPSSDVSE
RLQMFDDPRNKRGVIIKGLEEITVHNKDEVYQILEKGAAKRTTAATLMNAYSSRSHSVFS
VTIHMKETTIDGEELVKIGKLNLVDLAGSENIGRSGAVDKRAREAGNINQSLLTLGRVIT
ALVERTPHVPYRESKLTRILQDSLGGRTRTSIIATISPASLNLEETLSTLEYAHRAKNIL
NKPEVNQKL

Ligands and cofactors

ID	Name	Formula	Copies
PO4	Phosphate ion	O4 P	1
MG	Magnesium ion	Mg	2
ANP	Phosphoaminophosphonic acid-adenylate ester	C10 H17 N6 O12 P3	2

Primary citation

ATP Hydrolysis in Eg5 Kinesin Involves a Catalytic Two-water Mechanism. Parke, C.L., Wojcik, E.J., Kim, S. et al. J Biol Chem (2010) 285:5859-5867. DOI 10.1074/jbc.M109.071233 · PubMed

Other PDB entries of the same protein (UniProt P52732 (AlphaFold model), which also has an AlphaFold model), best resolution first:

3ZCW 1.69 Å, Eg5 - New allosteric binding site
6TLE 1.75 Å, Human Eg5 motor domain mutant E344K
1X88 1.8 Å, Human Eg5 motor domain bound to Mg-ADP and monastrol
6G6Y 1.8 Å, Eg5-inhibitor complex
2PG2 1.85 Å, Crystal structure of KSP in complex with ADP and thiophene containing inhibitor 15
1Q0B 1.9 Å, Crystal structure of the motor protein KSP in complex with ADP and monastrol
2X7C 1.9 Å, Crystal structure of human kinesin Eg5 in complex with (S)-enastron
8YHH 1.95 Å, The Crystal Structure of Mitotic Kinesin Eg5 from Biortus
3K5E 1.97 Å, The structure of human kinesin-like motor protein Kif11/KSP/Eg5 in complex with ADP and…
2WOG 2.0 Å, Intermediate and final states of human kinesin Eg5 in complex with S-trityl-L-cysteine
3L9H 2.0 Å, X-ray structure of mitotic kinesin-5 (KSP, KIF11, Eg5)in complex with the…
5JV3 2.01 Å, The neck-linker and alpha 7 helix of Homo sapiens Eg5 fused to EB1

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