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UniProt P04789

Triosephosphate isomerase, glycosomal (P04789)

Triosephosphate isomerase, glycosomal (UniProt P04789), EC 5.3.1.1: 92 experimental structures and 3 predicted models on GenesisL1, 5 ligands bound, 8 pockets. Binding sites, druggability and experiment against prediction…

UniProt
P04789
Protein
Triosephosphate isomerase, glycosomal
EC
5.3.1.1
Experimental structures
92
Predicted models
3
Ligands
5
Pockets
8 · 1 record with a druggable one

Structures

95 records of P04789 in the MolNFT archive: 92 experimental, 3 predicted.

EntryTitleMethodChainsLigandsPockets
1AG1Monohydrogen phosphate binding to trypanosomal triosephosphate isomerasex-ray diffractionO, T——
1AG1Monohydrogen phosphate binding to trypanosomal triosephosphate isomerasex-ray diffractionO, T——
1DKWCrystal structure of triose-phosphate isomerase with modified substrate binding sitex-ray diffractionA, B——
1DKWCrystal structure of triose-phosphate isomerase with modified substrate binding sitex-ray diffractionA, B——
1IIGStructure of trypanosoma brucei brucei triosephosphate isomerase complexed with…x-ray diffractionA, B——
1IIGStructure of trypanosoma brucei brucei triosephosphate isomerase complexed with…x-ray diffractionA, B——
1IIHStructure of trypanosoma brucei brucei triosephosphate isomerase complexed with 3-phosphoglyceratex-ray diffractionA, B——
1IIHStructure of trypanosoma brucei brucei triosephosphate isomerase complexed with 3-phosphoglyceratex-ray diffractionA, B——
1KV5Structure of Trypanosoma brucei brucei TIM with the salt-bridge-forming residue Arg191 mutated to…x-ray diffractionA, B——
1KV5Structure of trypanosoma brucei brucei tim with the salt-bridge- forming residue ARG191 mutated to…x-ray diffractionA, B——
1ML1Protein engineering with monomeric triosephosphate isomerase: the modelling and structure…x-ray diffractionA, C, E, G, I, K——
1ML1Protein engineering with monomeric triosephosphate isomerase: the modelling and structure…x-ray diffractionA, C, E, G, I, K——
1MSSLarge scale structural rearrangements of the front loops in monomerised triosephosphate isomerase…x-ray diffractionA, B——
1MSSLarge scale structural rearrangements of the front loops in monomerised triosephosphate isomerase…x-ray diffractionA, B——
1TPDStructures of the open" and "closed" state of trypanosomal triosephosphate isomerasex-ray diffractionA, B——
1TPDStructures of the "open" and "closed" state of trypanosomal triosephosphate isomerase, as observed…x-ray diffractionA, B——
1TPEComparison of the structures and the crystal contacts of trypanosomal triosephosphate isomerase in…x-ray diffractionA——
1TPEComparison of the structures and the crystal contacts of trypanosomal triosephosphate isomerase in…x-ray diffractionA——
1TPFComparison of the structures and the crystal contacts of trypanosomal triosephosphate isomerase in…x-ray diffractionA, B——
1TPFComparison of the structures and the crystal contacts of trypanosomal triosephosphate isomerase in…x-ray diffractionA, B——
1TRDThe influence of crystal packing on crystallographic binding studies: a new crystal form of…x-ray diffractionA, B——
1TRDThe influence of crystal packing on crystallographic binding studies: a new crystal form of…x-ray diffractionA, B——
1TRIThe crystal structure of an engineered monomeric triosephosphate isomerase, monotim: the correct…x-ray diffractionA——
1TRIThe crystal structure of an engineered monomeric triosephosphate isomerase, monotim: the correct…x-ray diffractionA——
1TSIStructure of the complex between trypanosomal triosephosphate isomerase and…x-ray diffractionA, B——
1TSIStructure of the complex between trypanosomal triosephosphate isomerase and N-hydroxy-4-phosphono…x-ray diffractionA, B——
1TTIThree new crystal structures of point mutation variants of monotim: conformational flexibility of…x-ray diffractionA——
1TTIThree new crystal structures of point mutation variants of monotim: conformational flexibility of…x-ray diffractionA——
1TTJThree new crystal structures of point mutation variants of monotim: conformational flexibility of…x-ray diffractionA——
1TTJThree new crystal structures of point mutation variants of monotim: conformational flexibility of…x-ray diffractionA——
2J24The functional role of the conserved active site proline of triosephosphate isomerasex-ray diffractionA, B——
2J24The functional role of the conserved active site proline of triosephosphate isomerasex-ray diffractionA, B——
2J27The functional role of the conserved active site proline of triosephosphate isomerase.x-ray diffractionA, B——
2J27The functional role of the conserved active site proline of triosephosphate isomerasex-ray diffractionA, B——
2V0TThe A178L mutation in the C-terminal hinge of the flexible loop-6 of triosephosphate isomerase…x-ray diffractionA, B, C, D, E, F, G, H——
2V0TThe A178L mutation in the C-terminal hinge of the flexible loop-6 of triosephosphate isomerase…x-ray diffractionA, B, C, D, E, F, G, H——
2V2CThe A178L mutation in the C-terminal hinge of the flexible loop-6 of triosephosphate isomerase…x-ray diffractionA——
2V2CThe A178L mutation in the C-terminal hinge of the flexible loop-6 of triosephosphate isomerase…x-ray diffractionA——
2V2DThe A178L mutation in the C-terminal hinge of the flexible loop-6 of triosephosphate isomerase…x-ray diffractionA——
2V2DThe A178L mutation in the C-terminal hinge of the flexible loop-6 of triosephosphate isomerase…x-ray diffractionA——
2V2HThe A178L mutation in the C-terminal hinge of the flexible loop-6 of triosephosphate isomerase…x-ray diffractionA, B, C——
2V2HThe A178L mutation in the C-terminal hinge of the flexible loop-6 of triosephosphate isomerase…x-ray diffractionA, B, C——
2V5LStructures of the Open and Closed State of Trypanosomal Triosephosphate Isomerase: as Observed in a…x-ray diffractionA, B——
2V5LStructures of the open and closed state of trypanosomal triosephosphate isomerase: as observed in a…x-ray diffractionA, B——
2VEIStructure-based enzyme engineering efforts with an inactive monomeric TIM variant: the importance…x-ray diffractionA, B, C——
2VEIStructure-based enzyme engineering efforts with an inactive monomeric tim variant: the importance…x-ray diffractionA, B, C——
2VEKStructure-based enzyme engineering efforts with an inactive monomeric TIM variant: the importance…x-ray diffractionA, B——
2VEKStructure-based enzyme engineering efforts with an inactive monomeric tim variant: the importance…x-ray diffractionA, B——
2VELStructure-based enzyme engineering efforts with an inactive monomeric TIM variant: the importance…x-ray diffractionA, B——
2VELStructure-based enzyme engineering efforts with an inactive monomeric tim variant: the importance…x-ray diffractionA, B——
2VEMStructure-based enzyme engineering efforts with an inactive monomeric TIM variant: the importance…x-ray diffractionA, B——
2VEMStructure-based enzyme engineering efforts with an inactive monomeric tim variant: the importance…x-ray diffractionA, B——
2VENStructure-based enzyme engineering efforts with an inactive monomeric TIM variant: the importance…x-ray diffractionA, B——
2VENStructure-based enzyme engineering efforts with an inactive monomeric tim variant: the importance…x-ray diffractionA, B——
2WSQMonoTIM mutant RMM0-1, dimeric form.x-ray diffractionA, B, C, D——
2WSQMonotim mutant RMM0-1, dimeric form.x-ray diffractionA, B, C, D——
2WSRMonotim mutant RMM0-1, monomeric form.x-ray diffractionA——
2WSRMonotim mutant RMM0-1, monomeric form.x-ray diffractionA——
2X16Crystallographic binding studies with an engineered monomeric variant of triosephosphate isomerasex-ray diffractionA, B——
2X16Crystallographic binding studies with an engineered monomeric variant of triosephosphate isomerasex-ray diffractionA, B——

35 records more on the page itself.

Ligands

  • G3P · Sn-glycerol-3-phosphate · in 1 record
  • K · Potassium ion · in 1 record
  • NA · Sodium ion · in 1 record
  • PGA · 2-phosphoglycolic acid · in 1 record
  • SO4 · Sulfate ion · in 1 record

Experiment against prediction

Elsewhere

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