Research workbench

Dntr inducer binding domain in complex with salicylate. trigonal crystal form

Analyse Dntr inducer binding domain in complex with salicylate. trigonal crystal form in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2Y7P
Type: protein
Length: 215 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Lysr-type regulatory protein
UniProt: Q7WT50
Ligands: SAL, PEU
Pockets: 1 · best druggability 0.68

Structure

x-ray diffraction · 1 distinct chain · 35% helix, 27% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Lysr-type regulatory protein	protein	215	35% helix, 27% strand	Q7WT50

Ligands and binding sites

SAL · 2-hydroxybenzoic acid · ligand · 2 copies · chains A
PEU · 2,5,8,11,14,17,20,23,26,29,32,35,38,41,44,47,50,53,56, 59,62,65,68,71,74,77,80-heptacosaoxadooctacontan-82-ol · ligand · 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	164	0.68	0.87	35	SAL, PEU

Compared structures

2Y7P · DntR Inducer Binding Domain in Complex with Salicylate. Trigonal crystal form · 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 Q7WT50
Elsewhere: RCSB PDB 2Y7P · PDBe 2Y7P · UniProt Q7WT50

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