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Novel dimerization motif in the dead box RNA helicase hera form 2, complete dimer, symmetric

Analyse Novel dimerization motif in the dead box RNA helicase hera form 2, complete… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3EAQ
Type: protein
Length: 416 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Heat resistant RNA dependent ATPase
UniProt: Q72GF3
Ligands: CL
Pockets: 2 · best druggability 0.37

Structure

x-ray diffraction · 2 distinct chains · 48% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Heat resistant RNA dependent ATPase	protein	207	49% helix, 15% strand	Q72GF3
B	Heat resistant RNA dependent ATPase	protein	209	47% helix, 16% strand	Q72GF3

Ligands and binding sites

CL · Chloride ion · ion · 2 copies · chains A, B

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

Pockets

2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	89	0.37	0.75	15	empty
2	56	0.30	0.75	16	empty

Interfaces

1 interface between chains.

A–B · 1581 Å² buried · 3 hydrogen bonds · protein-protein

Compared structures

3EAQ · Novel dimerization motif in the DEAD box RNA helicase Hera form 2, complete dimer… · the same entry in another collection · chain A against A, 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 Q72GF3
Elsewhere: RCSB PDB 3EAQ · PDBe 3EAQ · UniProt Q72GF3

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