2WOG: Kinesin-like protein KIF11

Intermediate and final states of human kinesin Eg5 in complex with S-trityl-L-cysteine. Determined by X-ray diffraction at 2.0 Å resolution. Released 4 Aug 2010.

Method: X-ray diffraction
Resolution: 2.0 Å
Organism: HOMO SAPIENS
Chains: 3
Atoms: 9,044
Mol. weight: 125.61 kDa
Ligands: ZZD, MG, ADP
Released: 4 Aug 2010

Explore 2WOG in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2WOG contains 66 α-helices and 61 β-strands across 3 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: 22 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
α-helix	37-38	2
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	98-105	8	2
α-helix	111-115	5
β-strand	117	1	5
α-helix	127-129	3
β-strand	133	1	5
α-helix	135-147	13
β-strand	153-164	12	2
β-strand	167-170	4	2
α-helix	180	1
β-strand	181	1	2
α-helix	182	1
β-strand	183-186	4	6
β-strand	194-197	4	6
β-strand	202-204	3	2
α-helix	207-209	3
α-helix	210-227	18
α-helix	231-234	4
β-strand	236-246	11	2
β-strand	248	1	7
β-strand	254	1	7
β-strand	257-265	9	2
α-helix	266-268	3
α-helix	290-304	15
α-helix	311-313	3
α-helix	315-320	6
α-helix	321-323	3
β-strand	329-336	8	2
β-strand	339	1	3
α-helix	340-342	3
α-helix	343-356	14
β-strand	360	1	1

Chain B: 21 helices, 19 β-strands

Element	Residues	Length	Sheet
β-strand	20-25	6	8
α-helix	26-28	3
α-helix	30-34	5
α-helix	37-38	2
β-strand	39	1	9
β-strand	41-44	4	10
β-strand	49-53	5	10
β-strand	63-67	5	10
β-strand	70-72	3	8
α-helix	78-81	4
α-helix	82-86	5
α-helix	87-94	8
β-strand	98-105	8	8
α-helix	111-115	5
β-strand	117	1	11
α-helix	119-120	2
β-strand	133	1	11
α-helix	135-150	16
β-strand	153-164	12	8
β-strand	167-170	4	8
α-helix	180	1
β-strand	181	1	8
α-helix	182	1
β-strand	183-186	4	12
β-strand	194-197	4	12
β-strand	202-204	3	8
α-helix	207-209	3
α-helix	210-225	16
α-helix	231-234	4
β-strand	236-246	11	8
β-strand	256-265	10	8
α-helix	266-268	3
α-helix	290-304	15
α-helix	311-313	3
α-helix	315-320	6
α-helix	321-323	3
β-strand	329-336	8	8
β-strand	339	1	9
α-helix	340-342	3
α-helix	343-356	14

Chain C: 23 helices, 19 β-strands

Element	Residues	Length	Sheet
β-strand	19-25	7	13
α-helix	26-28	3
α-helix	30-34	5
α-helix	37-38	2
β-strand	39	1	14
β-strand	41-44	4	15
β-strand	49-53	5	15
β-strand	63-67	5	15
β-strand	70-72	3	13
α-helix	78-81	4
α-helix	82-86	5
α-helix	87-94	8
β-strand	98-105	8	13
α-helix	111-115	5
β-strand	117	1	16
α-helix	119-120	2
α-helix	121-123	3
β-strand	133	1	16
α-helix	135-150	16
β-strand	153-164	12	13
β-strand	167-170	4	13
α-helix	180	1
β-strand	181	1	13
α-helix	182	1
β-strand	183-187	5	17
β-strand	190-197	8	17
β-strand	202-204	3	13
α-helix	207-209	3
α-helix	210-227	18
α-helix	231-234	4
β-strand	236-248	13	13
β-strand	254-265	12	13
α-helix	266-268	3
α-helix	290-303	14
α-helix	311-313	3
α-helix	315-320	6
α-helix	321-323	3
β-strand	330-336	7	13
β-strand	339	1	14
α-helix	340-342	3
α-helix	343-356	14
α-helix	359-361	3

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Kinesin-like protein KIF11	A, B, C	protein	368	HOMO SAPIENS	P52732 (AlphaFold model)

Sequence of entity 1 (A, B, C), FASTA

>2WOG_1 KINESIN-LIKE PROTEIN KIF11 (chains A, B, C)
MASQPNSSAKKKEEKGKNIQVVVRCRPFNLAERKASAHSIVECDPVRKEVSVRTGGLADK
SSRKTYTFDMVFGASTKQIDVYRSVVCPILDEVIMGYNCTIFAYGQTGTGKTFTMEGERS
PNEEYTWEEDPLAGIIPRTLHQIFEKLTDNGTEFSVKVSLLEIYNEELFDLLNPSSDVSE
RLQMFDDPRNKRGVIIKGLEEITVHNKDEVYQILEKGAAKRTTAATLMNAYSSRSHSVFS
VTIHMKETTIDGEELVKIGKLNLVDLAGSENIGRSGAVDKRAREAGNINQSLLTLGRVIT
ALVERTPHVPYRESKLTRILQDSLGGRTRTSIIATISPASLNLEETLSTLEYAHRAKNIL
NKPEVNQK

Ligands and cofactors

ID	Name	Formula	Copies
ZZD	S-trityl-L-cysteine	C22 H21 N O2 S	3
MG	Magnesium ion	Mg	3
ADP	Adenosine-5'-diphosphate	C10 H15 N5 O10 P2	3

Primary citation

An Allosteric Transition Trapped in an Intermediate State of a New Kinesin-Inhibitor Complex. Kaan, H.Y.K., Ulaganathan, V., Hackney, D.D. et al. Biochem J (2010) 425:55. DOI 10.1042/BJ20091207 · 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…
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
1II6 2.1 Å, Crystal Structure of the Mitotic Kinesin Eg5 in Complex with Mg-ADP.

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