6F1Z: Cytoplasmic dynein 1 intermediate chain 2

Roadblock-1 region of the dynein tail/dynactin/BICDR1 complex. Determined by electron microscopy at 3.4 Å resolution. Released 17 Jan 2018.

Method: Electron microscopy
Resolution: 3.4 Å
Organism: Homo sapiens
Chains: 4
Atoms: 2,138
Mol. weight: 158.75 kDa
Released: 17 Jan 2018

Explore 6F1Z in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6F1Z contains 9 α-helices and 12 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 o: 2 helices, 0 β-strands

Element	Residues	Length	Sheet
α-helix	184-191	8
α-helix	196-209	14

Chain p: 2 helices, 0 β-strands

Element	Residues	Length	Sheet
α-helix	187-192	6
α-helix	196-210	15

Chain s: 3 helices, 6 β-strands

Element	Residues	Length	Sheet
α-helix	4-10	7
β-strand	17-20	4	1
β-strand	21	1	2
β-strand	32	1	2
α-helix	36-41	6
α-helix	42-60	19
β-strand	66-73	8	1
β-strand	77-82	6	1
β-strand	87-92	6	1

Chain t: 2 helices, 6 β-strands

Element	Residues	Length	Sheet
α-helix	4-12	9
β-strand	17-19	3	1
β-strand	22	1	3
β-strand	31	1	3
α-helix	36-60	25
β-strand	66-73	8	1
β-strand	77-80	4	1
β-strand	89-92	4	1

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Cytoplasmic dynein 1 intermediate chain 2	o, p	protein	612	Homo sapiens	Q13409 (AlphaFold model)
Dynein light chain roadblock-type 1	s, t	protein	96	Homo sapiens	Q9NP97 (AlphaFold model)

Sequence of entity 1 (o, p), FASTA

>6F1Z_1 Cytoplasmic dynein 1 intermediate chain 2 (chains o, p)
MSDKSELKAELERKKQRLAQIREEKKRKEEERKKKETDQKKEAVAPVQEESDLEKKRREA
EALLQSMGLTPESPIVPPPMSPSSKSVSTPSEAGSQDSGDGAVGSRRGPIKLGMAKITQV
DFPPREIVTYTKETQTPVMAQPKEDEEEDDDVVAPKPPIEPEEEKTLKKDEENDSKAPPH
ELTEEEKQQILHSEEFLSFFDHSTRIVERALSEQINIFFDYSGRDLEDKEGEIQAGAKLS
LNRQFFDERWSKHRVVSCLDWSSQYPELLVASYNNNEDAPHEPDGVALVWNMKYKKTTPE
YVFHCQSAVMSATFAKFHPNLVVGGTYSGQIVLWDNRSNKRTPVQRTPLSAAAHTHPVYC
VNVVGTQNAHNLISISTDGKICSWSLDMLSHPQDSMELVHKQSKAVAVTSMSFPVGDVNN
FVVGSEEGSVYTACRHGSKAGISEMFEGHQGPITGIHCHAAVGAVDFSHLFVTSSFDWTV
KLWSTKNNKPLYSFEDNAGYVYDVMWSPTHPALFACVDGMGRLDLWNLNNDTEVPTASIS
VEGNPALNRVRWTHSGREIAVGDSEGQIVIYDVGEQIAVPRNDEWARFGRTLAEINANRA
DAEEEAATRIPA

Sequence of entity 2 (s, t), FASTA

>6F1Z_2 Dynein light chain roadblock-type 1 (chains s, t)
MAEVEETLKRLQSQKGVQGIIVVNTEGIPIKSTMDNPTTTQYASLMHSFILKARSTVRDI
DPQNDLTFLRIRSKKNEIMVAPDKDYFLIVIQNPTE

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 Q13409 (AlphaFold model), which also has an AlphaFold model), best resolution first:

7Z8I 3.3 Å, The barbed end complex of dynactin bound to BICDR1 and the cytoplasmic dynein tails (A2,…
6F1U 3.4 Å, N terminal region of dynein tail domains in complex with dynactin filament and BICDR-1
6F1T 3.5 Å, Cryo-EM structure of two dynein tail domains bound to dynactin and BICDR1
9BLY 3.5 Å, Composite structure of full-length human dynein-1 in phi-particle conformation
8PR2 3.8 Å, Cytoplasmic dynein-1 heavy chain bound to JIP3-LZI
8PR3 3.9 Å, Cytoplasmic dynein-1 heavy chain bound to JIP3-RH1
7Z8J 3.93 Å, Cytoplasmic dynein (A2) bound to BICDR1
9YNC 3.93 Å, Motor domains of phi-like human dynein-1 bound to dynactin-p150glued and LIS1
9YNG 4.07 Å, Dynactin and dynein-1 tail region of dynein-dynactin complex on microtubule in the…
8PQW 4.2 Å, Cytoplasmic dynein-1 motor domain bound to dynactin-p150glued and LIS1
9YND 4.26 Å, Motor domain of human dynein-1 in pre-power stroke bound to dynactin-p150glued-CC1B and…
7Z8K 4.37 Å, Cytoplasmic dynein (A1) bound to BICDR1

Browse structure collections

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