› 5x93

X-ray diffraction
2.2Å resolution

Human endothelin receptor type-B in complex with antagonist K-8794

Released:
DOI: 10.2210/pdb5x93/pdb
PDB entry 5x93 coloured by chain, front view.
PDB entry 5x93 coloured by chain, side view.
PDB entry 5x93 coloured by chain, top view.
Source organisms:
Primary publication:
X-ray structures of endothelin ETB receptor bound to clinical antagonist bosentan and its analog.
Shihoya W, Nishizawa T, Yamashita K, Inoue A, Hirata K, Kadji FMN, Okuta A, Tani K, Aoki J, Fujiyoshi Y, Doi T, Nureki O
Nat Struct Mol Biol 24 758-764 (2017)
PMID: 28805809

Function and Biology Details

Reaction catalysed: 
Hydrolysis of (1->4)-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrins
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-132967 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Endolysin; Endothelin receptor type B Chain: A
Molecule details ›
Chain: A
Length: 464 amino acids
Theoretical weight: 52.08 KDa
Source organisms: Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: P24530 (Residues: 66-303, 311-407; Coverage: 81%)
  • Canonical: P00720 (Residues: 61-161; Coverage: 62%)
Gene names: E, EDNRB, ETRB
Sequence domains:

Ligands and Environments

4 bound ligands:
Ligand K87 1 x K87
Ligand OLC 11 x OLC
Ligand CLR 1 x CLR
Ligand SO4 5 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL32XU
Spacegroup: C2221
Unit cell:
a: 74.13Å b: 147.48Å c: 108.38Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.212 0.211 0.239
Expression system: Spodoptera frugiperda

Quick links

Citations

6 review citations

Computer simulation of molecular recognition in biomolecular system: from in silico screening to generalized ensembles.
Fukunishi et al. (2022)
5 more

18 mentions without citation

Exploring G Protein-Coupled Receptors (GPCRs) Ligand Space via Cheminformatics Approaches: Impact on Rational Drug Design.
Basith et al. (2018)
17 more