6d67

X-ray diffraction
2.55Å resolution

Crystal structure of the human dual specificity phosphatase 1 catalytic domain (C258S) as a maltose binding protein fusion (maltose bound form) in complex with the designed AR protein mbp3_16

Released:
Primary publication:
MBP-binding DARPins facilitate the crystallization of an MBP fusion protein.
Acta Crystallogr F Struct Biol Commun 74 549-557 (2018)
PMID: 30198887

Function and Biology Details

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
PDBe Complex ID:
PDB-CPX-142531 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (3 distinct):
Dual specificity protein phosphatase 1; Maltose/maltodextrin-binding periplasmic protein Chain: A
Molecule details ›
Chain: A
Length: 520 amino acids
Theoretical weight: 57.1 KDa
Source organisms: Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P0AEX9 (Residues: 27-391; Coverage: 99%)
  • Canonical: P28562 (Residues: 172-314; Coverage: 39%)
Gene names: CL100, DUSP1, JW3994, MKP1, PTPN10, VH1, b4034, malE
Sequence domains:
Designed AR protein mbp3_16 Chain: B
Molecule details ›
Chain: B
Length: 136 amino acids
Theoretical weight: 14.79 KDa
Source organism: synthetic construct
Expression system: Escherichia coli BL21(DE3)
Structure domains: Ankyrin repeat-containing domain

Ligands and Environments

Carbohydrate polymer : NEW Components: GLC
3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007 HF
Spacegroup: P212121
Unit cell:
a: 75.286Å b: 84.699Å c: 105.962Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.185 0.182 0.252
Expression system: Escherichia coli BL21(DE3)