PDBsum entry 4d3r

Hydrolase

PDB id: 4d3r

Contents

Protein chain

140 a.a.

Ligands

SO4

Waters ×115

PDB id:

4d3r

Name:

Hydrolase

Title:

Crystal structure of point mutated dusp19 (i187a)

Structure:

Dual specificity protein phosphatase 19. Chain: a. Fragment: phosphatase domains, residues 65-204. Synonym: dual specificity phosphatase ts-dsp1, low molecular weight dual specificity phosphatase 3, lmw-dsp3, protein phosphatase skrp 1, stress-activated protein kinase pathway-regulating phosphatase 1, sapk pathway-regulating phosphatase 1. Engineered: yes. Mutation: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008

Resolution:

1.67Å R-factor: 0.163 R-free: 0.199

Authors:

T.J.Jeon,K.T.Nam,S.E.Ryu

Key ref:

T.J.Jeon et al. (2015). Structural analysis of activity-Modulating mutations dusp19. Biodesign, 3, 116.

Date:

23-Oct-14 Release date: 04-Nov-15

Protein chain

Q8WTR2  (DUS19_HUMAN) -  Dual specificity protein phosphatase 19 from Homo sapiens

Seq: 217 a.a.

Struc: 140 a.a.*

* PDB and UniProt seqs differ at 2 residue positions (black crosses)

Enzyme reactions

• Enzyme class 2: E.C.3.1.3.16 - protein-serine/threonine phosphatase.
• Reaction:
  1. O-phospho-L-seryl-[protein] + H2O = L-seryl-[protein] + phosphate
  2. O-phospho-L-threonyl-[protein] + H2O = L-threonyl-[protein] + phosphate
• Enzyme class 3: E.C.3.1.3.48 - protein-tyrosine-phosphatase.
• Reaction: O-phospho-L-tyrosyl-[protein] + H2O = L-tyrosyl-[protein] + phosphate

Note, where more than one E.C. class is given (as above), each may correspond to a different protein domain or, in the case of polyprotein precursors, to a different mature protein.

Molecule diagrams generated from .mol files obtained from the KEGG ftp site