Research workbench

DDX6

Analyse DDX6 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4CT5
Type: protein
Length: 750 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: DDX6
EC: 3.6.4.13
UniProt: P26196
Pockets: 10 · best druggability 0.66

Structure

x-ray diffraction · 1 distinct chain · 39% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	DDX6 (EC 3.6.4.13)	protein	375	39% helix, 17% strand	P26196

Ligands and binding sites

ACT · Acetate ion · additive · 2 copies · chains A, B

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

Pockets

10 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	709	0.66	0.75	72	empty
2	209	0.55	0.78	30	ACT
3	296	0.54	0.75	44	empty
4	117	0.53	0.83	19	empty
5	56	0.51	0.86	17	empty

Interfaces

1 interface between chains.

A–B · 1492 Å² buried · 16 hydrogen bonds · protein-protein

Compared structures

4CT5 · DDX6 · the same entry in another collection · chain A against A, TM-score 1.00
P26196 · AlphaFold monomer V2.0 prediction for probable ATP-dependent RNA helicase DDX6 (P26196) · a predicted model of the same protein · chain B against A, TM-score 0.54

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 P26196
Elsewhere: RCSB PDB 4CT5 · PDBe 4CT5 · UniProt P26196

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