Research workbench

Lasr-OC12 hsl complex

Analyse Lasr-OC12 hsl complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3IX3
Type: protein
Length: 326 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Transcriptional activator protein lasr
UniProt: P25084
Ligands: OHN
Pockets: 3 · best druggability 0.81

Structure

x-ray diffraction · 1 distinct chain · 53% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Transcriptional activator protein lasr	protein	163	53% helix, 17% strand	P25084

Ligands and binding sites

OHN · N-3-oxo-dodecanoyl-L-homoserine lactone · ligand · 2 copies · chains A, B

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

Pockets

3 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	167	0.81	0.97	31	OHN
2	169	0.80	0.96	31	OHN
3	170	0.51	0.78	29	empty

Interfaces

1 interface between chains.

A–B · 921 Å² buried · 9 hydrogen bonds · protein-protein

Compared structures

3IX3 · LasR-OC12 HSL complex · the same entry in another collection · chain A against A, TM-score 1.00
P25084 · AlphaFold monomer V2.0 prediction for transcriptional activator protein lasr (P25084) · a predicted model of the same protein · chain A against A, TM-score 0.98

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 P25084
Elsewhere: RCSB PDB 3IX3 · PDBe 3IX3 · UniProt P25084

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