› 6g1e

X-ray diffraction
1.88Å resolution

BEAT Fc with improved heterodimerization (Q3A-D84.4Q)

Released:
DOI: 10.2210/pdb6g1e/pdb
PDB entry 6g1e coloured by chain, front view.
PDB entry 6g1e coloured by chain, side view.
PDB entry 6g1e coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
A single mutation increases heavy-chain heterodimer assembly of bispecific antibodies by inducing structural disorder in one homodimer species.
Stutz C, Blein S
J Biol Chem 295 9392-9408 (2020)
PMID: 32404368

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-134811 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (3 distinct):
Immunoglobulin heavy constant gamma 1; Immunoglobulin heavy constant gamma 3 Chain: A
Molecule details ›
Chain: A
Length: 233 amino acids
Theoretical weight: 26.37 KDa
Source organism: Homo sapiens
Expression system: Homo sapiens
UniProt:
  • Canonical: P01860 (Residues: 151-151, 204-375; Coverage: 39%)
  • Canonical: P01857 (Residues: 105-156; Coverage: 13%)
Gene names: IGHG1, IGHG3
Sequence domains: Immunoglobulin C1-set domain
Structure domains: Immunoglobulins
Immunoglobulin gamma-1 heavy chain Chain: B
Molecule details ›
Chain: B
Length: 227 amino acids
Theoretical weight: 25.44 KDa
Source organism: Homo sapiens
Expression system: Homo sapiens
UniProt:
  • Canonical: P0DOX5 (Residues: 223-449; Coverage: 51%)
Sequence domains: Immunoglobulin C1-set domain
Structure domains: Immunoglobulins

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG, BMA, MAN, GAL, FUL
Carbohydrate polymer
No bound ligands
1 modified residue:
Ligand MLY 2 x MLY

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE MASSIF-1
Spacegroup: P212121
Unit cell:
a: 49.65Å b: 73.02Å c: 140.93Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.233 0.231 0.272
Expression system: Homo sapiens

Quick links

Citations

1 review citation

Ten years in the making: application of CrossMab technology for the development of therapeutic bispecific antibodies and antibody fusion proteins.
Surowka et al. (2021)
2 other articles

1 mention without citation

A single mutation increases heavy-chain heterodimer assembly of bispecific antibodies by inducing structural disorder in one homodimer species.
Stutz et al. (2020)