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Structure of H. salinarum rosr (VNG0258) grown from nacl

Analyse Structure of H. salinarum rosr (VNG0258) grown from nacl in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6F5C
Type: protein
Length: 220 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Halophilic winged-helix-turn-helix DNA binding protein
UniProt: Q9HSF4
Ligands: CL, SO4
Pockets: 1 · best druggability 0.81

Structure

x-ray diffraction · 1 distinct chain · 65% helix, 11% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Halophilic winged-helix-turn-helix DNA binding protein	protein	110	65% helix, 11% strand	Q9HSF4

Ligands and binding sites

CL · Chloride ion · ion · 25 copies · chains A, B
SO4 · Sulfate ion · ion · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	159	0.81	0.97	30	CL

Interfaces

1 interface between chains.

A–B · 2033 Å² buried · 18 hydrogen bonds · protein-protein

Compared structures

6F5C · Structure of h. salinarum RosR (vng0258) grown from NaCl · 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 Q9HSF4
Elsewhere: RCSB PDB 6F5C · PDBe 6F5C · UniProt Q9HSF4

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