› 3pnw

X-ray diffraction
2.05Å resolution

Crystal Structure of the tudor domain of human TDRD3 in complex with an anti-TDRD3 FAB

Released:
DOI: 10.2210/pdb3pnw/pdb
PDB entry 3pnw coloured by chain, front view.
PDB entry 3pnw coloured by chain, side view.
PDB entry 3pnw coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
CDR-H3 diversity is not required for antigen recognition by synthetic antibodies.
Persson H, Ye W, Wernimont A, Adams JJ, Koide A, Koide S, Lam R, Sidhu SS
J Mol Biol 425 803-11 (2013)
PMID: 23219464

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-212732 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
FAB light chain Chains: A, D, G, J, M, P, S, V
Molecule details ›
Chains: A, D, G, J, M, P, S, V
Length: 228 amino acids
Theoretical weight: 24.93 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
Structure domains: Immunoglobulins
FAB heavy chain Chains: B, E, H, K, N, Q, T, W
Molecule details ›
Chains: B, E, H, K, N, Q, T, W
Length: 246 amino acids
Theoretical weight: 26.13 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
Structure domains: Immunoglobulins
Tudor domain-containing protein 3 Chains: C, F, I, L, O, R, U, X
Molecule details ›
Chains: C, F, I, L, O, R, U, X
Length: 77 amino acids
Theoretical weight: 8.98 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9H7E2 (Residues: 540-615; Coverage: 12%)
Gene name: TDRD3
Sequence domains: Tudor domain
Structure domains: SH3 type barrels.

Ligands and Environments

1 bound ligand:
Ligand UNX 143 x UNX
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P1
Unit cell:
a: 76.708Å b: 93.726Å c: 159.932Å
α: 80.96° β: 82.82° γ: 90.06°
R-values:
R R work R free
0.224 0.223 0.264
Expression system: Escherichia coli

Quick links

Citations

9 review citations

Fc Engineering for Developing Therapeutic Bispecific Antibodies and Novel Scaffolds.
Liu et al. (2017)
8 more

5 mentions without citation

CDR-H3 diversity is not required for antigen recognition by synthetic antibodies.
Persson et al. (2013)
4 more