1II6: Mitotic Kinesin Eg5

Crystal Structure of the Mitotic Kinesin Eg5 in Complex with Mg-ADP. Determined by X-ray diffraction at 2.1 Å resolution. Released 18 Jul 2001.

Method
X-ray diffraction
Resolution
2.1 Å
Organism
Homo sapiens
Chains
2
Atoms
5,704
Mol. weight
83.14 kDa
Ligands
ADP, MG
Released
18 Jul 2001

Explore 1II6 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1II6 contains 37 α-helices and 36 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: 19 helices, 18 β-strands

ElementResiduesLengthSheet
β-strand19-2571
α-helix30-345
β-strand3912
β-strand41-4443
β-strand49-5353
β-strand63-6753
β-strand70-7231
α-helix78-814
α-helix82-865
α-helix87-948
β-strand98-10581
α-helix111-1155
β-strand11714
α-helix129-1302
β-strand13314
α-helix135-14915
β-strand153-164121
β-strand167-17041
β-strand183-18535
α-helix186-1872
β-strand195-19735
β-strand202-20431
α-helix207-2093
α-helix210-22617
α-helix232-2343
β-strand236-247121
β-strand255-265111
α-helix266-2683
α-helix282-30423
α-helix311-3133
α-helix315-3195
α-helix321-3244
β-strand330-33671
β-strand33912
α-helix340-3423
α-helix343-35614
α-helix360-3623
Chain B: 18 helices, 18 β-strands
ElementResiduesLengthSheet
β-strand19-2576
α-helix26-283
α-helix30-345
α-helix37-382
β-strand3917
β-strand41-4448
β-strand49-5358
β-strand63-6758
β-strand70-7236
α-helix78-814
α-helix82-865
α-helix87-948
β-strand98-10586
α-helix111-1155
β-strand11719
β-strand13319
α-helix135-14915
β-strand153-164126
β-strand167-17046
β-strand184-187410
β-strand190-196710
β-strand202-20436
α-helix209-22820
α-helix232-2343
β-strand236-247126
β-strand255-265116
α-helix266-2683
α-helix269-2713
α-helix291-30313
α-helix311-3133
α-helix315-3195
β-strand330-33676
β-strand33917
α-helix340-3423
α-helix343-35614
α-helix360-3634

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Kinesin-related motor protein Eg5A, Bprotein368Homo sapiensP52732 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>1II6_1 KINESIN-RELATED MOTOR PROTEIN Eg5 (chains A, B)
MASQPNSSAKKKEEKGKNIQVVVRCRPFNLAERKASAHSIVECDPVRKEVSVRTGGLADK
SSRKTYTFDMVFGASTKQIDVYRSVVCPILDEVIMGYNCTIFAYGQTGTGKTFTMEGERS
PNEEYTWEEDPLAGIIPRTLHQIFEKLTDNGTEFSVKVSLLEIYNEELFDLLNPSSDVSE
RLQMFDDPRNKRGVIIKGLEEITVHNKDEVYQILEKGAAKRTTAATLMNAYSSRSHSVFS
VTIHMKETTIDGEELVKIGKLNLVDLAGSENIGRSGAVDKRAREAGNINQSLLTLGRVIT
ALVERTPHVPYRESKLTRILQDSLGGRTRTSIIATISPASLNLEETLSTLEYAHRAKNIL
NKPEVNQK

Ligands and cofactors

IDNameFormulaCopies
ADPAdenosine-5'-diphosphateC10 H15 N5 O10 P22
MGMagnesium ionMg2

Water and common crystallization additives (NO3) are not listed.

Primary citation

Crystal structure of the mitotic spindle kinesin Eg5 reveals a novel conformation of the neck-linker. Turner, J., Anderson, R., Guo, J. et al. J Biol Chem (2001) 276:25496-25502. DOI 10.1074/jbc.M100395200 · PubMed

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

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