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Cryo-EM structure of two dynein tail domains bound to dynactin and BICDR1

Analyse Cryo-EM structure of two dynein tail domains bound to dynactin and BICDR1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6F1T
Type
protein
Length
13,986 residues
Chains
45
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
ARP1 actin related protein 1 homolog a; Actin, cytoplasmic 1; Actin related protein 10…
UniProt
F2Z5G5, Q6QAQ1, I3LHK5, A0PFK5, A9XFX6, D0G6S1, A0A286ZK88, A0JNT9, F1SKF9, Q14204, Q13409, O43237, Q9NP97
Ligands
ADP, ATP
Pockets
20 · best druggability 0.87

Structure

electron microscopy · 29 distinct chains · 52% helix, 10% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, D, E, F, G, IARP1 actin related protein 1 homolog aprotein37035% helix, 20% strandF2Z5G5
HActin, cytoplasmic 1protein37041% helix, 18% strandQ6QAQ1
JActin related protein 10 homologprotein36940% helix, 13% strandI3LHK5
KCapping protein (actin filament) muscle Z-line, alpha 1protein27840% helix, 25% strandA0PFK5
LF-actin capping protein beta subunitprotein26938% helix, 26% strandA9XFX6
MDynactin subunit 2protein58793% helix, 0% strand—
NDynactin subunit 2protein61690% helix, 0% strand—
O, PDynactin subunit 3protein6543% helix, 28% strand—
Q, RDynactin subunit 2protein8789% helix, 0% strand—
UDynactin 6protein17113% helix, 14% strandD0G6S1
VDynactin subunit 5protein1658% helix, 16% strandA0A286ZK88
XBicd family-like cargo adapter 1,BICD family-like cargo adapter 1,BICD family-like cargo adapter 1,BICDR-1protein28599% helix, 0% strandA0JNT9
YDynactin subunit 4protein26311% helix, 6% strand—
ZDynactin subunit 1protein5267% helix, 0% strand—
aDynactin subunit 2protein5221% helix, 12% strandF1SKF9
bDynactin subunit 2protein759% helix, 5% strandF1SKF9
cDynactin subunit 2protein3716% helix, 16% strandF1SKF9
dDynactin subunit 2protein2413% helix, 13% strandF1SKF9
e, mCytoplasmic dynein 1 heavy chain 1,CYTOPLASMIC dynein 1 heavy chain 1,CYTOPLASMIC dynein 1 heavy chain 1,DYNEIN heavy chain, cytoplasmic dynein 1 heavy chain 1,CYTOPLASMIC dynein 1 heavy chain 1,CYTOPLASMIC dynein 1 heavy chain 1,CYTOPLASMIC dynein 1 heavy chain 1,DYNEIN heavy CHAIN,CYTOPLASMIC dynein 1 heavy chain 1,CYTOPLASMIC dynein 1 heavy chain 1protein92667% helix, 2% strandQ14204
fCytoplasmic dynein 1 heavy chain 1,CYTOPLASMIC dynein 1 heavy chain 1,CYTOPLASMIC dynein 1 heavy chain 1,DYNEIN heavy chain, cytoplasmic dynein 1 heavy chain 1,CYTOPLASMIC dynein 1 heavy chain 1,CYTOPLASMIC dynein 1 heavy chain 1,CYTOPLASMIC dynein 1 heavy chain 1,DYNEIN heavy CHAIN,CYTOPLASMIC dynein 1 heavy chain 1,CYTOPLASMIC dynein 1 heavy chain 1protein92966% helix, 4% strandQ14204
g, oCytoplasmic dynein 1 intermediate chain 2protein39710% helix, 28% strandQ13409
hCytoplasmic dynein 1 intermediate chain 2protein4008% helix, 27% strandQ13409
i, q, rCytoplasmic dynein 1 light intermediate chain 2protein26841% helix, 11% strandO43237
jCytoplasmic dynein 1 light intermediate chain 2protein28835% helix, 11% strandO43237
k, l, s, tDynein light chain roadblock-type 1protein9335% helix, 16% strandQ9NP97
nCytoplasmic dynein 1 heavy chain 1,CYTOPLASMIC dynein 1 heavy chain 1,CYTOPLASMIC dynein 1 heavy chain 1,DYNEIN heavy chain, cytoplasmic dynein 1 heavy chain 1,CYTOPLASMIC dynein 1 heavy chain 1,CYTOPLASMIC dynein 1 heavy chain 1,CYTOPLASMIC dynein 1 heavy chain 1,DYNEIN heavy CHAIN,CYTOPLASMIC dynein 1 heavy chain 1,CYTOPLASMIC dynein 1 heavy chain 1protein92867% helix, 4% strandQ14204
pCytoplasmic dynein 1 intermediate chain 2protein4019% helix, 25% strandQ13409
xBicd family-like cargo adapter 1,BICD family-like cargo adapter 1,BICD family-like cargo adapter 1protein28899% helix, 0% strandA0JNT9
zDynactin subunit 1protein5372% helix, 0% strand—

Ligands and binding sites

  • ADP · Adenosine-5'-diphosphate · ligand · 9 copies · chains A, B, C, a, D, E, F, G, I, J
  • ATP · Adenosine-5'-triphosphate · ligand · chains H

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
19920.870.88105empty
29280.850.86107ADP
38910.850.8790empty
420740.850.86248empty
521110.840.85198empty

Interfaces

105 interfaces between chains.

  • K–L · 3802 Ų buried · 53 hydrogen bonds · protein-protein
  • X–x · 3557 Ų buried · 16 hydrogen bonds · protein-protein
  • f–h · 1841 Ų buried · 23 hydrogen bonds · protein-protein
  • G–b · 1614 Ų buried · 11 hydrogen bonds · protein-protein
  • m–o · 1557 Ų buried · 16 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 6 covalent (covalent ligand).

Compared structures

  • 6F1T · Cryo-EM structure of two dynein tail domains bound to dynactin and BICDR1 · the same entry in another collection · chain K against K, TM-score 1.00

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