Research workbench

Crystal Structure of the C-terminal Ligand-Binding Domain of the LysR family Transcriptional Regulator YfbA from Yersinia pestis

Analyse Crystal Structure of the C-terminal Ligand-Binding Domain of the LysR family… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7TRW
Type: protein
Length: 213 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 2.28
Source: Yersinia pestis CO92
Molecule: LysR-family transcriptional regulatory protein
UniProt: Q8D0G2
Ligands: 3HB, PO4
Pockets: 1 · best druggability 0.71

Structure

x-ray diffraction · resolution 2.28 · 1 distinct chain · 32% helix, 32% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	LysR-family transcriptional regulatory protein	protein	213	32% helix, 32% strand	Q8D0G2

Ligands and binding sites

3HB · 3-hydroxybenzoic acid · ligand · chains A
PO4 · Phosphate 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	466	0.71	0.81	49	3HB, PO4

Modifications

Observed in the structure: 5 modified (engineered).

Compared structures

7TRW · Crystal structure of the C-terminal ligand-binding domain of the lysr family… · 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 Q8D0G2
Elsewhere: RCSB PDB 7TRW · PDBe 7TRW · UniProt Q8D0G2

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.