› 1xdt

X-ray diffraction
2.65Å resolution

COMPLEX OF DIPHTHERIA TOXIN AND HEPARIN-BINDING EPIDERMAL GROWTH FACTOR

Released:
DOI: 10.2210/pdb1xdt/pdb
PDB entry 1xdt coloured by chain, front view.
PDB entry 1xdt coloured by chain, side view.
PDB entry 1xdt coloured by chain, top view.
Source organisms:
Primary publication:
Crystal structure of the complex of diphtheria toxin with an extracellular fragment of its receptor.
Louie GV, Yang W, Bowman ME, Choe S
Mol Cell 1 67-78 (1997)
PMID: 9659904

Function and Biology Details

Reaction catalysed: 
NAD(+) + diphthamide-[translation elongation factor 2] = nicotinamide + N-(ADP-D-ribosyl)diphthamide-[translation elongation factor 2]
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-132744 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Diphtheria toxin Chain: T
Molecule details ›
Chain: T
Length: 535 amino acids
Theoretical weight: 58.41 KDa
Source organism: Corynebacterium diphtheriae
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P00588 (Residues: 33-567; Coverage: 100%)
Sequence domains:
Structure domains:
Heparin-binding EGF-like growth factor Chain: R
Molecule details ›
Chain: R
Length: 79 amino acids
Theoretical weight: 8.93 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q99075 (Residues: 72-147; Coverage: 40%)
Gene names: DTR, DTS, HBEGF, HEGFL
Structure domains: Laminin

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: C2221
Unit cell:
a: 89.4Å b: 103.7Å c: 127.7Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.172 0.172 0.29
Expression system: Escherichia coli BL21

Quick links

Citations

8 review citations

3D domain swapping: as domains continue to swap.
Liu et al. (2002)
7 more

18 mentions without citation

ADP-ribosylation systems in bacteria and viruses.
Mikolčević et al. (2021)
17 more