MolNFT v1 · #164568 · protein
Lmrp from L. lactis, in an outward-open conformation, bound to hoechst 33342
6T1Z: “Lmrp from L. lactis, in an outward-open conformation, bound to hoechst 33342”. X-ray diffraction, 3 ligands (XP4, LMU, HT1). MolNFT v1 #164568 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6T1Z
- Type
- protein
- Length
- 393 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q48658
- Ligands
- XP4, LMU, HT1
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 393 | — | 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.
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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