› 6my4

X-ray diffraction
1.69Å resolution

Crystal structure of the dimeric bH1-Fab variant [HC-Y33W,HC-D98M,HC-G99M,LC-S30bR]

Released:
DOI: 10.2210/pdb6my4/pdb
PDB entry 6my4 coloured by chain, front view.
PDB entry 6my4 coloured by chain, side view.
PDB entry 6my4 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Binding symmetry and surface flexibility mediate antibody self-association.
Schrag JD, Picard MÈ, Gaudreault F, Gagnon LP, Baardsnes J, Manenda MS, Sheff J, Deprez C, Baptista C, Hogues H, Kelly JF, Purisima EO, Shi R, Sulea T
OpenAccess logo MAbs 11 1300-1318 (2019)
PMID: 31318308

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-182258 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Ig-like domain-containing protein Chains: A, H
Molecule details ›
Chains: A, H
Length: 236 amino acids
Theoretical weight: 25.42 KDa
Source organism: Homo sapiens
Expression system: Cricetulus griseus
UniProt:
  • Canonical: V9HW68 (Residues: 20-246; Coverage: 50%)
Gene name: HEL-214
Sequence domains:
Ig-like domain-containing protein Chains: B, L
Molecule details ›
Chains: B, L
Length: 218 amino acids
Theoretical weight: 24.03 KDa
Source organism: Homo sapiens
Expression system: Cricetulus griseus
UniProt:
  • Canonical: Q7Z3Y4 (Residues: 23-51, 52-236; Coverage: 100%)
Sequence domains:

Ligands and Environments

1 bound ligand:
Ligand EDO 6 x EDO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: CLSI BEAMLINE 08ID-1
Spacegroup: P21
Unit cell:
a: 81.869Å b: 65.86Å c: 93.13Å
α: 90° β: 99.93° γ: 90°
R-values:
R R work R free
0.191 0.189 0.23
Expression system: Cricetulus griseus

Quick links

Citations

2 review citations

Assessing developability early in the discovery process for novel biologics.
Fernández-Quintero et al. (2023)
1 more

1 mention without citation

Binding symmetry and surface flexibility mediate antibody self-association.
Schrag et al. (2019)