› 2vxn

X-ray diffraction
0.82Å resolution

E65Q-TIM complexed with phosphoglycolohydroxamate at 0.82 A resolution

Released:
DOI: 10.2210/pdb2vxn/pdb
PDB entry 2vxn coloured by chain, front view.
PDB entry 2vxn coloured by chain, side view.
PDB entry 2vxn coloured by chain, top view.
Source organism: Leishmania mexicana
Primary publication:
Atomic resolution crystallography of a complex of triosephosphate isomerase with a reaction-intermediate analog: new insight in the proton transfer reaction mechanism.
Alahuhta M, Wierenga RK
Proteins 78 1878-88 (2010)
PMID: 20235230

Function and Biology Details

Reaction catalysed: 
D-glyceraldehyde 3-phosphate = glycerone phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-155741 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Triosephosphate isomerase Chain: A
Molecule details ›
Chain: A
Length: 251 amino acids
Theoretical weight: 27.21 KDa
Source organism: Leishmania mexicana
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P48499 (Residues: 1-251; Coverage: 100%)
Sequence domains: Triosephosphate isomerase
Structure domains: Aldolase class I

Ligands and Environments

4 bound ligands:
Ligand PGH 1 x PGH
Ligand PGA 1 x PGA
Ligand GOL 5 x GOL
Ligand ACT 1 x ACT
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE BW7B
Spacegroup: C2
Unit cell:
a: 98.36Å b: 50.65Å c: 58.66Å
α: 90° β: 117.56° γ: 90°
R-values:
R R work R free
0.092 not available 0.103
Expression system: Escherichia coli BL21

Quick links

Citations

1 review citation

Triosephosphate isomerase: a highly evolved biocatalyst.
Wierenga et al. (2010)
9 other articles

16 mentions without citation

A role for flexible loops in enzyme catalysis.
Malabanan et al. (2010)
15 more