› 5i3f

X-ray diffraction
1.72Å resolution

Structure-Function Studies on Role of Hydrophobic Clamping of a Basic Glutamate in Catalysis by Triosephosphate Isomerase

Released:
DOI: 10.2210/pdb5i3f/pdb
PDB entry 5i3f coloured by chain, front view.
PDB entry 5i3f coloured by chain, side view.
PDB entry 5i3f coloured by chain, top view.
Source organism: Trypanosoma brucei brucei
Primary publication:
Structure-Function Studies of Hydrophobic Residues That Clamp a Basic Glutamate Side Chain during Catalysis by Triosephosphate Isomerase.
Richard JP, Amyes TL, Malabanan MM, Zhai X, Kim KJ, Reinhardt CJ, Wierenga RK, Drake EJ, Gulick AM
Biochemistry 55 3036-47 (2016)
PMID: 27149328

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-138176 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Triosephosphate isomerase, glycosomal Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 250 amino acids
Theoretical weight: 26.82 KDa
Source organism: Trypanosoma brucei brucei
Expression system: Escherichia coli
UniProt:
  • Canonical: P04789 (Residues: 1-250; Coverage: 100%)
Sequence domains: Triosephosphate isomerase
Structure domains: Aldolase class I

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL7-1
Spacegroup: P21
Unit cell:
a: 70.847Å b: 87.9Å c: 74.848Å
α: 90° β: 106.01° γ: 90°
R-values:
R R work R free
0.189 0.187 0.227
Expression system: Escherichia coli

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Citations

4 review citations

Enzyme activation through the utilization of intrinsic dianion binding energy.
Amyes et al. (2017)
3 more

1 mention without citation

Structure-Function Studies of Hydrophobic Residues That Clamp a Basic Glutamate Side Chain during Catalysis by Triosephosphate Isomerase.
Richard et al. (2016)