1G8X: Genetically engineered molecular motor

Structure of a genetically engineered molecular motor. Determined by X-ray diffraction at 2.8 Å resolution. Released 17 Jan 2001.

Method: X-ray diffraction
Resolution: 2.8 Å
Organism: Dictyostelium discoideum
Chains: 2
Atoms: 16,292
Mol. weight: 231.32 kDa
Ligands: ADP, MG
Released: 17 Jan 2001

Explore 1G8X in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1G8X contains 100 α-helices and 58 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: 48 helices, 28 β-strands

Element	Residues	Length	Sheet
α-helix	10-15	6
β-strand	34-37	4	1
β-strand	48-56	9	1
β-strand	59-63	5	1
β-strand	69-73	5	1
β-strand	79	1	1
α-helix	80-82	3
α-helix	83-85	3
β-strand	90	1	2
α-helix	91-93	3
α-helix	99-110	12
β-strand	116-119	4	2
β-strand	122-126	5	2
α-helix	137-143	7
α-helix	155-169	15
β-strand	173-179	7	2
α-helix	185-200	16
α-helix	210-226	17
β-strand	227-228	2	3
β-strand	236-237	2	3
β-strand	240-247	8	2
β-strand	253-261	9	2
α-helix	265-268	4
β-strand	278	1	3
α-helix	279-287	9
α-helix	290-296	7
α-helix	301-303	3
α-helix	305-307	3
β-strand	316	1	4
α-helix	320-334	15
α-helix	338-354	17
β-strand	360	1	5
β-strand	368	1	5
α-helix	373-382	10
α-helix	386-394	9
β-strand	397-399	3	6
β-strand	404-406	3	6
α-helix	412-441	30
β-strand	448-454	7	2
β-strand	464	1	7
α-helix	466-496	31
α-helix	511-518	8
α-helix	525-532	8
α-helix	540-551	12
β-strand	558-559	2	7
β-strand	567-572	6	7
β-strand	575-580	6	7
α-helix	584-589	6
α-helix	594-600	7
α-helix	606-613	8
α-helix	615-618	4
α-helix	630-645	16
β-strand	649-656	8	2
α-helix	669-678	10
α-helix	681-688	8
β-strand	694-697	4	8
α-helix	698-705	8
α-helix	706-708	3
α-helix	719-729	11
α-helix	734-736	3
β-strand	737-739	3	8
β-strand	743-746	4	8
α-helix	750-790	41
α-helix	798-813	16
α-helix	816-838	23
α-helix	843-845	3
α-helix	853-904	52
α-helix	906-909	4
α-helix	922-924	3
α-helix	928-931	4
α-helix	937-940	4
α-helix	942-955	14
α-helix	961-971	11
α-helix	972-976	5
α-helix	977-982	6
α-helix	984-987	4

Chain B: 52 helices, 30 β-strands

Element	Residues	Length	Sheet
α-helix	3-5	3
α-helix	10-14	5
β-strand	34-37	4	9
β-strand	48-52	5	9
β-strand	59-63	5	9
β-strand	70-73	4	9
β-strand	79	1	9
α-helix	80-82	3
α-helix	83-85	3
β-strand	90	1	10
α-helix	91-93	3
α-helix	99-110	12
β-strand	116-119	4	10
β-strand	122-126	5	10
α-helix	137-142	6
α-helix	155-169	15
β-strand	173-179	7	10
α-helix	185-200	16
α-helix	208-210	3
α-helix	211-226	16
β-strand	227-228	2	11
β-strand	236-237	2	11
β-strand	240-247	8	10
β-strand	253-261	9	10
α-helix	265-268	4
β-strand	278	1	11
α-helix	279-287	9
α-helix	290-293	4
α-helix	301-303	3
β-strand	316	1	4
α-helix	320-334	15
α-helix	338-356	19
β-strand	360-361	2	12
β-strand	367-368	2	12
α-helix	373-382	10
α-helix	386-394	9
α-helix	396	1
β-strand	397	1	13
α-helix	398	1
β-strand	406	1	13
α-helix	411-441	31
β-strand	448-454	7	10
β-strand	464	1	14
α-helix	466-495	30
α-helix	496-498	3
α-helix	510-518	9
α-helix	524	1
α-helix	525-532	8
α-helix	540-551	12
β-strand	558-559	2	14
β-strand	567-572	6	14
β-strand	575-580	6	14
α-helix	584-587	4
α-helix	594-601	8
α-helix	606-613	8
α-helix	615-618	4
β-strand	622	1	15
β-strand	627	1	15
α-helix	630-645	16
β-strand	649-656	8	10
α-helix	669-678	10
α-helix	681-688	8
β-strand	694-697	4	16
α-helix	698-705	8
α-helix	706-708	3
α-helix	719-729	11
β-strand	737-739	3	16
β-strand	743-746	4	16
α-helix	750-789	40
α-helix	798-811	14
α-helix	816-839	24
α-helix	847-848	2
α-helix	853-902	50
α-helix	904-906	3
α-helix	908-910	3
α-helix	918-924	7
α-helix	927-934	8
α-helix	936-939	4
α-helix	941-953	13
α-helix	961-971	11
α-helix	975-1003	29
α-helix	1005-1008	4

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Myosin II heavy chain fused to alpha-actinin 3	A, B	protein	1010	Dictyostelium discoideum	P05095 (AlphaFold model), P08799 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>1G8X_1 MYOSIN II HEAVY CHAIN FUSED TO ALPHA-ACTININ 3 (chains A, B)
MNPIHDRTSDYHKYLKVKQGDSDLFKLTVSDKRYIWYNPDPDERDSYECGEIVSETSDSF
TFKTVDGQDRQVKKDDANQRNPIKFDGVEDMSELSYLNEPAVFHNLRVRYNQDLIYTYSG
LFLVAVNPFKRIPIYTQEMVDIFKGRRRNEVAPHIFAISDVAYRSMLDDRQNQSLLITGE
SGAGKTENTKKVIQYLASVAGRNQANGSGVLEQQILQANPILEAFGNAKTTRNNNSSEFG
KFIEIQFNNAGFISGASIQSYLLEKSRVVFQSETERNYHIFYQLLAGATAEEKKALHLAG
PESFNYLNQSGCVDIKGVSDEDEFKITRQAMDIVGFSQEEQMSIFKIIAGILHLGNIKFE
KGAGEGAVLKDKTALNAASTVFGVNPSVLEKALMEPRILAGRDLVAQHLNVEKSSSSRDA
LVKALYGRLFLWLVKKINNVLCSERKAYFIGVLDISGFEIFKVNSFEQLCINYTNEKLQQ
FFNHHMFKVEQEEYLKEKINWTFIDFGLDSQATIDLIDGRQPPGILALLDEQSVFPNATD
NTLITKLHSHFSKKNAKYEEPRFSKTEFGVTHYAGQVMYEIQDWLEKNKDPLQQDLELCF
KDSSDNVVTKLFNDPNIASRAKKGANFITVAAQYKEQLASLMATLETTNPHFVRCIIPNN
KQLPAKLEDKVVLDQLRCNGVLEGIRITRKGFPNRIIYADFVKRYYLLAPNVPRDAEDSQ
KATDAVLKHLNIDPEQYRFGITKIFFRAGQLARIEEAREQRLGSEQTKSDYLKRANELVQ
WINDKQASLESRDFGDSIESVQSFMNAHKEYKKTEKPPKGQEVSELEAIYNSLQTKLRLI
KREPFVAPAGLTPNEIDSTWSALEKAEQEHAEALRIELKRQKKIAVLLQKYNRILKKLEN
WATTKSVYLGSNETGDSITAVQAKLKNLEAFDGECQSLEGQSNSDLLSILAQLTELNYNG
VPELTERKDTFFAQQWTGVKSSAETYKNTLLAELERLQKIEDLHHHHHHH

Ligands and cofactors

ID	Name	Formula	Copies
ADP	Adenosine-5'-diphosphate	C10 H15 N5 O10 P2	2
MG	Magnesium ion	Mg	2

Primary citation

Structure of a genetically engineered molecular motor. Kliche, W., Fujita-Becker, S., Kollmar, M. et al. EMBO J (2001) 20:40-46. DOI 10.1093/emboj/20.1.40 · PubMed

Other PDB entries of the same protein (UniProt P05095 (AlphaFold model), which also has an AlphaFold model), best resolution first:

9IHL 2.02 Å, Crystal Structure of the Human Nonmuscle Myosin 2A Motor Domain
5I4E 2.25 Å, Crystal Structure of Human Nonmuscle Myosin 2C motor domain
4PD3 2.84 Å, Crystal Structure of Rigor-Like Human Nonmuscle Myosin-2B
5JLH 3.9 Å, Cryo-EM structure of a human cytoplasmic actomyosin complex at near-atomic resolution

Browse structure collections

About this viewer

MolViewer shows 1G8X directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.