5OWO: Cytoplasmic dynein 1 heavy chain 1

Human cytoplasmic Dynein N-Terminus dimerization domain at 1.8 Angstrom resolution. Determined by X-ray diffraction at 1.79 Å resolution. Released 11 Jul 2018.

Method: X-ray diffraction
Resolution: 1.79 Å
Organism: Homo sapiens
Chains: 4
Atoms: 5,380
Mol. weight: 90.19 kDa
Ligands: CA, MG
Released: 11 Jul 2018

Explore 5OWO in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5OWO contains 40 α-helices and 24 β-strands across 4 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: 10 helices, 6 β-strands

Element	Residues	Length	Sheet
β-strand	24	1	1
α-helix	25-26	2
α-helix	27-41	15
α-helix	48-49	2
α-helix	50-57	8
α-helix	59-70	12
β-strand	76-85	10	2
β-strand	97-104	8	2
β-strand	113-120	8	2
β-strand	126	1	1
α-helix	132-134	3
β-strand	135-140	6	2
α-helix	145-152	8
α-helix	153-157	5
α-helix	158-165	8
α-helix	178-199	22

Chain B: 10 helices, 6 β-strands

Element	Residues	Length	Sheet
β-strand	24	1	3
α-helix	25-26	2
α-helix	27-41	15
α-helix	48-49	2
α-helix	50-57	8
α-helix	59-70	12
β-strand	76-84	9	4
β-strand	98-104	7	4
β-strand	113-120	8	4
β-strand	126	1	3
α-helix	132-134	3
β-strand	135-140	6	4
α-helix	145-152	8
α-helix	153-157	5
α-helix	158-166	9
α-helix	179-198	20

Chain C: 10 helices, 6 β-strands

Element	Residues	Length	Sheet
β-strand	24	1	5
α-helix	25-26	2
α-helix	27-41	15
α-helix	48-49	2
α-helix	50-57	8
α-helix	59-70	12
β-strand	76-84	9	4
β-strand	98-104	7	4
β-strand	113-120	8	4
β-strand	126	1	5
α-helix	132-134	3
β-strand	135-140	6	4
α-helix	145-152	8
α-helix	153-157	5
α-helix	158-166	9
α-helix	179-199	21

Chain D: 10 helices, 6 β-strands

Element	Residues	Length	Sheet
β-strand	24	1	6
α-helix	25-26	2
α-helix	27-41	15
α-helix	48-49	2
α-helix	50-57	8
α-helix	59-70	12
β-strand	76-84	9	2
β-strand	98-104	7	2
β-strand	113-120	8	2
β-strand	126	1	6
α-helix	132-134	3
β-strand	135-140	6	2
α-helix	145-152	8
α-helix	153-157	5
α-helix	158-165	8
α-helix	179-198	20

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Cytoplasmic dynein 1 heavy chain 1	A, B, C, D	protein	201	Homo sapiens	Q14204

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

>5OWO_1 Cytoplasmic dynein 1 heavy chain 1 (chains A, B, C, D)
MSEPGGGGGEDGSAGLEVSAVQNVADVSVLQKHLRKLVPLLLEDGGEAPAALEAALEEKS
ALEQMRKFLSDPQVHTVLVERSTLKEDVGDEGEEEKEFISYNINIDIHYGVKSNSLAFIK
RTPVIDADKPVSSQLRVLTLSEDSPYETLHSFISNAVAPFFKSYIRESGKADRDGDKMAP
SVEKKIAELEMGLLHLQQNIE

Ligands and cofactors

ID	Name	Formula	Copies
CA	Calcium ion	Ca	2
MG	Magnesium ion	Mg	26

Water and common crystallization additives (NA, K, GOL) are not listed.

Primary citation

Cryo-EM shows how dynactin recruits two dyneins for faster movement. Urnavicius, L., Lau, C.K., Elshenawy, M.M. et al. Nature (2018) 554:202-206. DOI 10.1038/nature25462 · PubMed

Other PDB entries of the same protein (UniProt Q14204), best resolution first:

9BLZ 2.2 Å, State-1(phi motor) of full-length human dynein-1 in 5mM ATP
9BMR 2.6 Å, State-1 of motor domain from full-length human phi dynein-1 in 5 mM ADP
9DH5 2.6 Å, State-1 of the motor domain from full-length human dynein-1 in 5mM AMPPNP with 5mM Mg2+
9E0X 2.7 Å, Cryo-EM structure of Phi dynein
9E10 2.71 Å, Dimeric motor domains from phi dynein-1 under Lis1 condition
9BM0 2.8 Å, State-2 of motor domain from full-length human dynein-1 in 5mM ATP
9BMF 2.8 Å, State-1(phi motor) of full-length human dynein-1 in 5mM ATPVi
9BMH 2.8 Å, State-4 of motor domain from full-length human dynein-1 in 5mM ATPVi
9BN3 2.8 Å, The alpha registry-locked dynein motor domain mutant in 5mM ATP condition, class1
9BM2 2.82 Å, State-4 of motor domain from full-length human dynein-1 in 5 mM ATP
9BMG 2.86 Å, State-2 of full-length human dynein-1 in 5mM ATPVi
9BMY 2.86 Å, State-1 of motor domain from full-length human dynein-1 in apo condition

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