Research workbench

Lmrp from L. lactis, in an outward-open conformation, bound to hoechst 33342

Analyse Lmrp from L. lactis, in an outward-open conformation, bound to hoechst 33342 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6T1Z
Type: protein
Length: 393 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Lmrp integral membrane protein
UniProt: Q48658
Ligands: XP4, LMU, HT1
Pockets: 1 · best druggability 0.80

Structure

x-ray diffraction · 1 distinct chain · 84% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Lmrp integral membrane protein	protein	393	84% helix, 0% strand	Q48658

Ligands and binding sites

XP4 · 1,2-dimyristoyl-sn-glycero-3-phosphate · ligand · 2 copies · chains A
LMU · Dodecyl-alpha-D-maltoside · ligand · 2 copies · chains A
HT1 · 2'-(4-ethoxyphenyl)-5-(4-methyl-1-piperazinyl)-2,5'-bi-benzimidazole · ligand · chains A
GOL · Glycerol · additive · 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	1095	0.80	0.81	76	HT1, XP4, LMU

Compared structures

6T1Z · LmrP from L. lactis, in an outward-open conformation, bound to Hoechst 33342 · 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 Q48658
Elsewhere: RCSB PDB 6T1Z · PDBe 6T1Z · UniProt Q48658

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