› 6cbv

X-ray diffraction
1.87Å resolution

Crystal structure of BRIL bound to an affinity matured synthetic antibody.

Released:
DOI: 10.2210/pdb6cbv/pdb
Model geometry
Fit model/data
PDB entry 6cbv coloured by chain, front view.
PDB entry 6cbv coloured by chain, side view.
PDB entry 6cbv coloured by chain, top view.
Source organisms:
Primary publication:
Synthetic antibodies against BRIL as universal fiducial marks for single-particle cryoEM structure determination of membrane proteins.
Mukherjee S, Erramilli SK, Ammirati M, Alvarez FJD, Fennell KF, Purdy MD, Skrobek BM, Radziwon K, Coukos J, Kang Y, Dutka P, Gao X, Qiu X, Yeager M, Eric Xu H, Han S, Kossiakoff AA
OpenAccess logo Nat Commun 11 1598 (2020)
PMID: 32221310

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-230830 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Heavy chain, Fab fragment Chain: H
Molecule details ›
Chain: H
Length: 229 amino acids
Theoretical weight: 24.32 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
Light Chain, Fab fragment Chain: L
Molecule details ›
Chain: L
Length: 214 amino acids
Theoretical weight: 23.35 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
Structure domains: Immunoglobulins
Soluble cytochrome b562 Chain: B

Ligands and Environments

3 bound ligands:
Ligand GOL 2 x GOL
Ligand FMT 2 x FMT
Ligand NA 1 x NA
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: APS BEAMLINE 24-ID-C
Spacegroup: P65
Unit cell:
a: 87.954Å b: 87.954Å c: 159.107Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.195 0.194 0.225
Expression system: Escherichia coli

Quick links

Citations

8 review citations

Exploring cellular biochemistry with nanobodies.
Cheloha et al. (2020)
7 more

5 mentions without citation

Structure of human Frizzled5 by fiducial-assisted cryo-EM supports a heterodimeric mechanism of canonical Wnt signaling.
Tsutsumi et al. (2020)
4 more