› 1ml1

X-ray diffraction
2.6Å resolution

PROTEIN ENGINEERING WITH MONOMERIC TRIOSEPHOSPHATE ISOMERASE: THE MODELLING AND STRUCTURE VERIFICATION OF A SEVEN RESIDUE LOOP

Released:
DOI: 10.2210/pdb1ml1/pdb
PDB entry 1ml1 coloured by chain, front view.
PDB entry 1ml1 coloured by chain, side view.
PDB entry 1ml1 coloured by chain, top view.
Source organism: Trypanosoma brucei brucei
Primary publication:
Protein engineering with monomeric triosephosphate isomerase (monoTIM): the modelling and structure verification of a seven-residue loop.
Thanki N, Zeelen JP, Mathieu M, Jaenicke R, Abagyan RA, Wierenga RK, Schliebs W
Protein Eng 10 159-67 (1997)
PMID: 9089815

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-138176 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Triosephosphate isomerase, glycosomal Chains: A, C, E, G, I, K
Molecule details ›
Chains: A, C, E, G, I, K
Length: 243 amino acids
Theoretical weight: 26.14 KDa
Source organism: Trypanosoma brucei brucei
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P04789 (Residues: 1-250; Coverage: 97%)
Sequence domains: Triosephosphate isomerase
Structure domains: Aldolase class I

Ligands and Environments

1 bound ligand:
Ligand PGA 6 x PGA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X11
Spacegroup: P3
Unit cell:
a: 165.23Å b: 165.23Å c: 51.23Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.231 0.231 0.247
Expression system: Escherichia coli BL21(DE3)

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Citations

6 review citations

Comparative protein structure modeling of genes and genomes.
Martí-Renom et al. (2000)
5 more

4 mentions without citation

The Potential of Secondary Metabolites from Plants as Drugs or Leads against Protozoan Neglected Diseases-Part III: In-Silico Molecular Docking Investigations.
Ogungbe et al. (2016)
3 more