MolNFT v1 · #62274 · protein

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

3EAQ · Heat resistant RNA dependent ATPase: “Novel dimerization motif in the dead box RNA helicase hera form 2, complete dimer, symmetric”. X-ray diffraction, 1 ligand (CL), 2 pockets (best druggability 0.37). MolNFT v1 #62274 on…

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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