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C terminal region of the dynein heavy chains in the dynein TAIL/DYNACTIN/BICDR1 complex

Analyse C terminal region of the dynein heavy chains in the dynein TAIL/DYNACTIN/BICDR1… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6F1V
Type: protein
Length: 628 residues
Chains: 2
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cytoplasmic dynein 1 heavy chain 1
UniProt: Q14204
Pockets: 7 · best druggability 0.65

Structure

electron microscopy · 2 distinct chains · 74% helix, 1% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
f	Cytoplasmic dynein 1 heavy chain 1	protein	411	74% helix, 1% strand	Q14204
m	Cytoplasmic dynein 1 heavy chain 1	protein	217	75% helix, 0% strand	Q14204

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	154	0.65	0.86	28	empty
2	174	0.46	0.75	25	empty
3	90	0.46	0.80	20	empty
4	54	0.31	0.76	16	empty
5	69	0.30	0.74	13	empty

Interfaces

1 interface between chains.

f–m · 362 Å² buried · 2 hydrogen bonds · protein-protein

Compared structures

6F1V · C terminal region of the dynein heavy chains in the dynein tail/dynactin/BICDR1 complex · the same entry in another collection · chain f against f, TM-score 1.00

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt Q14204
Elsewhere: RCSB PDB 6F1V · PDBe 6F1V · UniProt Q14204

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