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Engineering the ptpbeta catalytic domain with improved crystallization properties

Analyse Engineering the ptpbeta catalytic domain with improved crystallization… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2I5X
Type
protein
Length
561 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Receptor-type tyrosine-protein phosphatase beta
EC
3.1.3.48
UniProt
P23467
Ligands
UA5, MG, CL

Structure

x-ray diffraction · 2 distinct chains · 39% helix, 22% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AReceptor-type tyrosine-protein phosphatase beta (EC 3.1.3.48)protein28038% helix, 22% strandP23467
BReceptor-type tyrosine-protein phosphatase beta (EC 3.1.3.48)protein28140% helix, 22% strandP23467

Ligands and binding sites

  • UA5 · (4-ethylphenyl)sulfamic acid · ligand · 2 copies · chains A, B
  • MG · Magnesium ion · metal · chains B
  • CL · Chloride ion · ion · 2 copies · chains A, B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Interfaces

1 interface between chains.

  • A–B · 87 Ų buried · 3 hydrogen bonds · protein-protein

Compared structures

  • 2I5X · Engineering the PTPbeta catalytic domain with improved crystallization properties · the same entry in another collection · chain A against A, TM-score 1.00
  • P23467 · AlphaFold monomer V2.0 prediction for receptor-type tyrosine-protein phosphatase beta… · a predicted model of the same protein · chain B against A, TM-score 0.99

Analyse

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