Research workbench

Lasr lbd L130F:3OC10HSL complex

Analyse Lasr lbd L130F:3OC10HSL complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6MVN
Type: protein
Length: 324 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Transcriptional regulator lasr
UniProt: A0A0H2Z901
Ligands: 3M5
Pockets: 5 · best druggability 0.81

Structure

x-ray diffraction · 1 distinct chain · 54% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Transcriptional regulator lasr	protein	162	54% helix, 17% strand	A0A0H2Z901

Ligands and binding sites

3M5 · 3-oxo-N-[(3S)-2-oxotetrahydrofuran-3-yl]decanamide · ligand · 2 copies · chains A, B

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

Pockets

5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	161	0.81	0.96	29	3M5
2	147	0.81	0.97	28	3M5
3	247	0.50	0.75	38	empty
4	65	0.41	0.81	20	empty
5	73	0.35	0.76	16	empty

Interfaces

1 interface between chains.

A–B · 830 Å² buried · 3 hydrogen bonds · protein-protein

Compared structures

6MVN · LasR LBD L130F:3OC10HSL complex · 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 A0A0H2Z901
Elsewhere: RCSB PDB 6MVN · PDBe 6MVN · UniProt A0A0H2Z901

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