PDBsum entry 3py2

Isomerase

PDB id: 3py2

Contents

Protein chains

246 a.a.

Ligands

SO4 ×2

EDO

Waters ×622

PDB id:

3py2

Name:

Isomerase

Title:

Structure of c126s mutant of plasmodium falciparum triosephosphate isomerase

Structure:

Triosephosphate isomerase. Chain: a, b. Synonym: tim, triose-phosphate isomerase. Engineered: yes. Mutation: yes

Source:

Plasmodium falciparum. Organism_taxid: 5833. Gene: tpi. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

1.93Å R-factor: 0.175 R-free: 0.220

Authors:

M.Samanta,M.Banerjee,M.R.N.Murthy,H.Balaram,P.Balaram

Key ref:

M.Samanta et al. (2011). Probing the role of the fully conserved Cys126 in triosephosphate isomerase by site-specific mutagenesis--distal effects on dimer stability. Febs J, 278, 1932-1943. PubMed id: 21447068

Date:

11-Dec-10 Release date: 27-Apr-11

Protein chains

Q07412  (TPIS_PLAFA) -  Triosephosphate isomerase from Plasmodium falciparum

Seq: 248 a.a.

Struc: 246 a.a.*

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

Enzyme reactions

• Enzyme class: E.C.5.3.1.1 - triose-phosphate isomerase.
• Reaction: D-glyceraldehyde 3-phosphate = dihydroxyacetone phosphate

D-glyceraldehyde 3-phosphate (Bound ligand (Het Group name = EDO) matches with 40.00% similarity) = dihydroxyacetone phosphate

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

Added reference

Febs J 278:1932-1943 (2011)

PubMed id: 21447068

Probing the role of the fully conserved Cys126 in triosephosphate isomerase by site-specific mutagenesis--distal effects on dimer stability.

M.Samanta, M.Banerjee, M.R.Murthy, H.Balaram, P.Balaram.

ABSTRACT

No abstract given.