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Almost closed conformation of the helicase core of the RNA helicase hera

Analyse Almost closed conformation of the helicase core of the RNA helicase hera in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4KBG
Type: protein
Length: 572 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Heat resistant RNA dependent ATPase
UniProt: Q72GF3
Ligands: SO4
Pockets: 4 · best druggability 0.73

Structure

x-ray diffraction · 2 distinct chains · 42% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Heat resistant RNA dependent ATPase	protein	207	45% helix, 14% strand	Q72GF3
B	Heat resistant RNA dependent ATPase	protein	365	41% helix, 18% strand	Q72GF3

Ligands and binding sites

SO4 · Sulfate ion · ion · 6 copies · chains A, B

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

Pockets

4 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	912	0.73	0.77	90	SO4
2	148	0.44	0.75	20	empty
3	119	0.38	0.74	27	empty
4	93	0.35	0.74	18	empty

Interfaces

1 interface between chains.

A–B · 857 Å² buried · 6 hydrogen bonds · protein-protein

Compared structures

4KBG · almost closed conformation of the helicase core of the RNA helicase Hera · 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 4KBG · PDBe 4KBG · UniProt Q72GF3

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