5tsr

X-ray diffraction
3.19Å resolution

Crystal structure of PRL-3 phosphatase in complex with the Bateman domain of CNNM3 magnesium transporter

Released:

Function and Biology Details

Reaction catalysed:
Protein tyrosine phosphate + H(2)O = protein tyrosine + phosphate
Biochemical function:
Cellular component:

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Protein tyrosine phosphatase type IVA 3 Chains: A, C
Molecule details ›
Chains: A, C
Length: 172 amino acids
Theoretical weight: 19.38 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: O75365 (Residues: 1-169; Coverage: 98%)
Gene names: PRL3, PTP4A3
Sequence domains: Dual specificity phosphatase, catalytic domain
Metal transporter CNNM3 Chains: B, D
Molecule details ›
Chains: B, D
Length: 155 amino acids
Theoretical weight: 17.63 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q8NE01 (Residues: 309-452; Coverage: 20%)
Gene names: ACDP3, CNNM3
Sequence domains: CBS domain

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: CHESS BEAMLINE F1
Spacegroup: C2
Unit cell:
a: 155.339Å b: 125.146Å c: 52.042Å
α: 90° β: 102.21° γ: 90°
R-values:
R R work R free
0.241 0.239 0.287
Expression system: Escherichia coli BL21