1W9I: Myosin II heavy chain

Myosin II Dictyostelium discoideum motor domain S456Y bound with MgADP-BeFx. Determined by X-ray diffraction at 1.75 Å resolution. Released 16 Mar 2006.

Method
X-ray diffraction
Resolution
1.75 Å
Organism
DICTYOSTELIUM DISCOIDEUM
Chains
1
Atoms
6,489
Mol. weight
89.33 kDa
Ligands
BEF, ADP, MG
Released
16 Mar 2006

Explore 1W9I in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1W9I contains 31 α-helices and 27 β-strands across 1 chain. 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: 31 helices, 27 β-strands

ElementResiduesLengthSheet
α-helix10-156
β-strand34-3741
β-strand48-5581
β-strand59-6351
β-strand69-7351
β-strand78-7921
α-helix80-823
α-helix83-853
β-strand9012
α-helix91-933
α-helix99-11113
β-strand116-11942
β-strand122-12652
α-helix137-1437
α-helix148-1503
α-helix155-16915
β-strand173-17862
α-helix185-20016
α-helix210-22617
β-strand227-22823
β-strand236-23723
β-strand240-24782
β-strand253-26192
α-helix265-2684
β-strand27813
α-helix279-2879
α-helix290-2967
α-helix301-3033
α-helix320-33415
α-helix338-35518
β-strand360-36124
β-strand367-36824
α-helix373-38210
α-helix386-3949
β-strand397-40045
β-strand403-40645
α-helix411-44131
β-strand448-45472
α-helix466-49530
α-helix506-5105
α-helix511-5188
α-helix525-5339
α-helix540-55112
β-strand558-55926
β-strand567-57266
β-strand575-58066
α-helix584-5896
α-helix594-6018
α-helix608-6136
α-helix615-6184
β-strand622-62327
β-strand626-62727
α-helix630-64617
β-strand649-65682
α-helix669-67810
α-helix681-6877
β-strand694-69748
β-strand743-74648

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Myosin II heavy chainAprotein770DICTYOSTELIUM DISCOIDEUMP08799 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>1W9I_1 MYOSIN II HEAVY CHAIN (chains A)
MNPIHDRTSDYHKYLKVKQGDSDLFKLTVSDKRYIWYNPDPKERDSYECGEIVSETSDSF
TFKTVDGQDRQVKKDDANQRNPIKFDGVEDMSELSYLNEPAVFHNLRVRYNQDLIYTYSG
LFLVAVNPFKRIPIYTQEMVDIFKGRRRNEVAPHIFAISDVAYRSMLDDRQNQSLLITGE
SGAGKTENTKKVIQYLASVAGRNQANGSGVLEQQILQANPILEAFGNAKTTRNNNSSRFG
KFIEIQFNSAGFISGASIQSYLLEKSRVVFQSETERNYHIFYQLLAGATAEEKKALHLAG
PESFNYLNQSGCVDIKGVSDSEEFKITRQAMDIVGFSQEEQMSIFKIIAGILHLGNIKFE
KGAGEGAVLKDKTALNAASTVFGVNPSVLEKALMEPRILAGRDLVAQHLNVEKSSSSRDA
LVKALYGRLFLWLVKKINNVLCQERKAYFIGVLDIYGFEIFKVNSFEQLCINYTNEKLQQ
FFNHHMFKLEQEEYLKEKINWTFIDFGLDSQATIDLIDGRQPPGILALLDEQSVFPNATD
NTLITKLHSHFSKKNAKYEEPRFSKTEFGVTHYAGQVMYEIQDWLEKNKDPLQQDLELCF
KDSSDNVVTKLFNDPNIASRAKKGANFITVAAQYKEQLASLMATLETTNPHFVRCIIPNN
KQLPAKLEDKVVLDQLRCNGVLEGIRITRKGFPNRIIYADFVKRYYLLAPNVPRDAEDSQ
KATDAVLKHLNIDPEQFRFGITKIFFRAGQLARIEEARELRGDYKDDDDK

Ligands and cofactors

IDNameFormulaCopies
BEFBeryllium trifluoride ionBe F31
ADPAdenosine-5'-diphosphateC10 H15 N5 O10 P21
MGMagnesium ionMg1

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

Primary citation

Structure-Function Analysis of Myosin II Backdoor Mutants. Morris, C.A., Coureux, P.-D., Wells, A.L. et al. To be published.

Other PDB entries of the same protein (UniProt P08799 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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