1tpe

COMPARISON OF THE STRUCTURES AND THE CRYSTAL CONTACTS OF TRYPANOSOMAL TRIOSEPHOSPHATE ISOMERASE IN FOUR DIFFERENT CRYSTAL FORMS

Method: X-RAY DIFFRACTION D_max: 55.2 Å Quality: GOOD

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1. Protein Identity and Related Structures Protein Identity & Related Structures

TRIOSEPHOSPHATE ISOMERASE

Trypanosoma brucei brucei

State in the Current Structure

Assembly	Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Associated Components	Method and Experimental Conditions	Structure Quality
1	Protein homooligomer Homooligomer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain A； UniProt 1–250	Not recorded	No other associated polymer	X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions	Resolution 2.10 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

Other PDB	Difference from Current Entry 1TPE	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1AG1 MONOHYDROGEN PHOSPHATE BINDING TO TRYPANOSOMAL TRIOSEPHOSPHATE ISOMERASE Deposited 1997-03-28	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain O 1–250（250 aa） Chain T 1–250（250 aa）	Not recorded	PO4 PHOSPHATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 7；2.4 M AMMONIUM SULFATE IN 0.2 MOPS BUFFER, PH 7.0 FOLLOWED BY TRANSFER TO 44% PEG-6000 CONTAINING 15 MM PHOSPHATE	Resolution 2.36 Å
1DKW CRYSTAL STRUCTURE OF TRIOSE-PHOSPHATE ISOMERASE WITH MODIFIED SUBSTRATE BINDING SITE Deposited 1999-12-08	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 2–250（249 aa） Chain B 2–250（249 aa）	Not recorded	TBU TERTIARY-BUTYL ALCOHOL × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.5；277 K；1.0 M CITRIC ACID PH 6.5, 20% PEG6000, 2.5% T-BUTANOL, pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 2.65 Å R-free 0.242
1IIG STRUCTURE OF TRYPANOSOMA BRUCEI BRUCEI TRIOSEPHOSPHATE ISOMERASE COMPLEXED WITH 3-PHOSPHONOPROPIONATE Deposited 2001-04-23	Different construct Different mutation/modification Different ligand/ion Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–250（250 aa） Chain B 1–250（250 aa）	Not recorded	3PP 3-PHOSPHONOPROPANOIC ACID × 1	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.60 Å
1IIH STRUCTURE OF TRYPANOSOMA BRUCEI BRUCEI TRIOSEPHOSPHATE ISOMERASE COMPLEXED WITH 3-PHOSPHOGLYCERATE Deposited 2001-04-23	Different construct Different mutation/modification Different ligand/ion Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–250（250 aa） Chain B 1–250（250 aa）	Not recorded	3PG 3-PHOSPHOGLYCERIC ACID × 1	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.20 Å
1KV5 Structure of Trypanosoma brucei brucei TIM with the salt-bridge-forming residue Arg191 mutated to Ser Deposited 2002-01-25	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–250（250 aa） Chain B 1–250（250 aa）	Mutation：R191S Mutation：R191S	PGA 2-PHOSPHOGLYCOLIC ACID × 2 DTT 2,3-DIHYDROXY-1,4-DITHIOBUTANE × 1 GOL GLYCEROL × 4 SO4 SULFATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.5；295 K；ammonium sulfate, sodium chloride, citric acid, pH 5.5, VAPOR DIFFUSION, HANGING DROP at 295K	Resolution 1.65 Å R-free 0.175
1ML1 PROTEIN ENGINEERING WITH MONOMERIC TRIOSEPHOSPHATE ISOMERASE: THE MODELLING AND STRUCTURE VERIFICATION OF A SEVEN RESIDUE LOOP Deposited 1996-09-27	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–250（250 aa） Chain C 1–250（250 aa）	Not recorded	PGA 2-PHOSPHOGLYCOLIC ACID × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 7.5；PLEASE SEE JRNL ARTICLE, pH 7.5	Resolution 2.60 Å R-free 0.247
1ML1 PROTEIN ENGINEERING WITH MONOMERIC TRIOSEPHOSPHATE ISOMERASE: THE MODELLING AND STRUCTURE VERIFICATION OF A SEVEN RESIDUE LOOP Deposited 1996-09-27	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain E 1–250（250 aa） Chain G 1–250（250 aa）	Not recorded	PGA 2-PHOSPHOGLYCOLIC ACID × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 7.5；PLEASE SEE JRNL ARTICLE, pH 7.5	Resolution 2.60 Å R-free 0.247
1ML1 PROTEIN ENGINEERING WITH MONOMERIC TRIOSEPHOSPHATE ISOMERASE: THE MODELLING AND STRUCTURE VERIFICATION OF A SEVEN RESIDUE LOOP Deposited 1996-09-27	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain I 1–250（250 aa） Chain K 1–250（250 aa）	Not recorded	PGA 2-PHOSPHOGLYCOLIC ACID × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 7.5；PLEASE SEE JRNL ARTICLE, pH 7.5	Resolution 2.60 Å R-free 0.247
1MSS LARGE SCALE STRUCTURAL REARRANGEMENTS OF THE FRONT LOOPS IN MONOMERISED TRIOSEPHOSPHATE ISOMERASE, AS DEDUCED FROM THE COMPARISON OF THE STRUCTURAL PROPERTIES OF MONOTIM AND ITS POINT MUTATION VARIANT MONOSS Deposited 1994-07-27	Different construct Different mutation/modification Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–250（250 aa） Chain B 1–250（250 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.40 Å
1TPD STRUCTURES OF THE "OPEN" AND "CLOSED" STATE OF TRYPANOSOMAL TRIOSEPHOSPHATE ISOMERASE, AS OBSERVED IN A NEW CRYSTAL FORM: IMPLICATIONS FOR THE REACTION MECHANISM Deposited 1994-02-28	Parsed fields agree	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–250（250 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.10 Å
1TPD STRUCTURES OF THE "OPEN" AND "CLOSED" STATE OF TRYPANOSOMAL TRIOSEPHOSPHATE ISOMERASE, AS OBSERVED IN A NEW CRYSTAL FORM: IMPLICATIONS FOR THE REACTION MECHANISM Deposited 1994-02-28	Different oligomeric state	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 1–250（250 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.10 Å
1TPD STRUCTURES OF THE "OPEN" AND "CLOSED" STATE OF TRYPANOSOMAL TRIOSEPHOSPHATE ISOMERASE, AS OBSERVED IN A NEW CRYSTAL FORM: IMPLICATIONS FOR THE REACTION MECHANISM Deposited 1994-02-28	Parsed fields agree	Assembly 3 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain B 1–250（250 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.10 Å
1TPF COMPARISON OF THE STRUCTURES AND THE CRYSTAL CONTACTS OF TRYPANOSOMAL TRIOSEPHOSPHATE ISOMERASE IN FOUR DIFFERENT CRYSTAL FORMS Deposited 1994-02-28	Different construct Different mutation/modification Different ligand/ion Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–250（250 aa） Chain B 1–250（250 aa）	Not recorded	DMS DIMETHYL SULFOXIDE × 4	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 1.80 Å
1TRD THE INFLUENCE OF CRYSTAL PACKING ON CRYSTALLOGRAPHIC BINDING STUDIES: A NEW CRYSTAL FORM OF TRYPANOSOMAL TIM Deposited 1992-10-06	Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–250（250 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.50 Å
1TRD THE INFLUENCE OF CRYSTAL PACKING ON CRYSTALLOGRAPHIC BINDING STUDIES: A NEW CRYSTAL FORM OF TRYPANOSOMAL TIM Deposited 1992-10-06	Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 1–250（250 aa）	Not recorded	PGH PHOSPHOGLYCOLOHYDROXAMIC ACID × 1	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.50 Å
1TRD THE INFLUENCE OF CRYSTAL PACKING ON CRYSTALLOGRAPHIC BINDING STUDIES: A NEW CRYSTAL FORM OF TRYPANOSOMAL TIM Deposited 1992-10-06	Different ligand/ion Different structure-quality metrics	Assembly 3 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain B 1–250（250 aa）	Not recorded	PGH PHOSPHOGLYCOLOHYDROXAMIC ACID × 2	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.50 Å
1TRI THE CRYSTAL STRUCTURE OF AN ENGINEERED MONOMERIC TRIOSEPHOSPHATE ISOMERASE, MONOTIM: THE CORRECT MODELLING OF AN EIGHT-RESIDUE LOOP Deposited 1993-10-08	Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–250（250 aa）	Not recorded	SO4 SULFATE ION × 1	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.40 Å
1TSI STRUCTURE OF THE COMPLEX BETWEEN TRYPANOSOMAL TRIOSEPHOSPHATE ISOMERASE AND N-HYDROXY-4-PHOSPHONO-BUTANAMIDE: BINDING AT THE ACTIVE SITE DESPITE AN "OPEN" FLEXIBLE LOOP Deposited 1992-11-19	Different construct Different mutation/modification Different ligand/ion Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–250（250 aa） Chain B 1–250（250 aa）	Not recorded	4PB N-HYDROXY-4-PHOSPHONO-BUTANAMIDE × 1	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.84 Å
1TTI THREE NEW CRYSTAL STRUCTURES OF POINT MUTATION VARIANTS OF MONOTIM: CONFORMATIONAL FLEXIBILITY OF LOOP-1,LOOP-4 AND LOOP-8 Deposited 1995-04-19	Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–250（250 aa）	Mutation：I68G, A69N, K70A, S71D, DEL(73-79), P81A, A100W	PGA 2-PHOSPHOGLYCOLIC ACID × 1	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.40 Å
1TTJ THREE NEW CRYSTAL STRUCTURES OF POINT MUTATION VARIANTS OF MONOTIM: CONFORMATIONAL FLEXIBILITY OF LOOP-1,LOOP-4 AND LOOP-8 Deposited 1995-04-20	Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–250（250 aa）	Mutation：VARIANT OF MONOTIM WITH PHE 45 REPLACED BY SER AND VAL 46 REPLACED BY SER (F45S, V46S) AND 73 - 79 DELETED	PGH PHOSPHOGLYCOLOHYDROXAMIC ACID × 1	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.40 Å
2J24 The functional role of the conserved active site proline of triosephosphate isomerase Deposited 2006-08-16	Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–250（250 aa） Chain B 1–250（250 aa）	Mutation：YES Mutation：YES	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 7；WELL SOLUTION: 0.1 M TEA PH 7.0, 27% PEG 2K MME AND 0.2 M KSCN PROTEIN SOLUTION: 11 MG/ML PROTEIN, 0.02 M TRIS/HCL PH 7.0, 0.1 M NACL, 1 MM DTT, 1 MM EDTA AND 1 MM NAN3.	Resolution 2.10 Å R-free 0.230
2J27 The functional role of the conserved active site proline of triosephosphate isomerase. Deposited 2006-08-16	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–250（250 aa） Chain B 1–250（250 aa）	Mutation：YES Mutation：YES	PGA 2-PHOSPHOGLYCOLIC ACID × 2 SO4 SULFATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 9.5；WELL SOLUTION: 0.1 M CHES PH 9.5, 25 % PEG 1500, 200 MM MGSO4 PROTEIN SOLUTION: 11.5 MG/ML PROTEIN, 20 MM TRIS/HCL PH 7, 100 MM NACL, 1 MM DTT, 1 MM EDTA, 1 MM NAN3 AND 10 MM 2PG	Resolution 1.15 Å R-free 0.190
2V0T The A178L mutation in the C-terminal hinge of the flexible loop-6 of triosephosphate isomerase (TIM) induces a more closed conformation of this hinge region in dimeric and monomeric TIM Deposited 2007-05-18	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–250（250 aa） Chain B 1–250（250 aa）	Mutation：YES Mutation：YES	SO4 SULFATE ION × 3	X-RAY DIFFRACTION X-ray crystallization conditions pH 7.5；0.1 M HEPES PH 7.5, 8% ETHYLENE GLYCOL AND 10% PEG8000	Resolution 2.20 Å R-free 0.238
2V0T The A178L mutation in the C-terminal hinge of the flexible loop-6 of triosephosphate isomerase (TIM) induces a more closed conformation of this hinge region in dimeric and monomeric TIM Deposited 2007-05-18	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain C 1–250（250 aa） Chain E 1–250（250 aa）	Mutation：YES Mutation：YES	SO4 SULFATE ION × 3 EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 7.5；0.1 M HEPES PH 7.5, 8% ETHYLENE GLYCOL AND 10% PEG8000	Resolution 2.20 Å R-free 0.238
2V0T The A178L mutation in the C-terminal hinge of the flexible loop-6 of triosephosphate isomerase (TIM) induces a more closed conformation of this hinge region in dimeric and monomeric TIM Deposited 2007-05-18	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain D 1–250（250 aa） Chain F 1–250（250 aa）	Mutation：YES Mutation：YES	SO4 SULFATE ION × 2 EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 7.5；0.1 M HEPES PH 7.5, 8% ETHYLENE GLYCOL AND 10% PEG8000	Resolution 2.20 Å R-free 0.238
2V0T The A178L mutation in the C-terminal hinge of the flexible loop-6 of triosephosphate isomerase (TIM) induces a more closed conformation of this hinge region in dimeric and monomeric TIM Deposited 2007-05-18	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 4 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain G 1–250（250 aa） Chain H 1–250（250 aa）	Mutation：YES Mutation：YES	SO4 SULFATE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 7.5；0.1 M HEPES PH 7.5, 8% ETHYLENE GLYCOL AND 10% PEG8000	Resolution 2.20 Å R-free 0.238
2V2C The A178L mutation in the C-terminal hinge of the flexible loop-6 of triosephosphate isomerase (TIM) induces a more closed conformation of this hinge region in dimeric and monomeric TIM Deposited 2007-06-05	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–250（250 aa）	Mutation：YES	SO4 SULFATE ION × 6 PGA 2-PHOSPHOGLYCOLIC ACID × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 7.5；0.1 M TEA PH 7.5, 2 % PEG 400, 2.0 M (NH4)2SO4	Resolution 1.89 Å R-free 0.182
2V2D The A178L mutation in the C-terminal hinge of the flexible loop-6 of triosephosphate isomerase (TIM) induces a more closed conformation of this hinge region in dimeric and monomeric TIM Deposited 2007-06-05	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 1–13（13 aa） Chain A 15–72（58 aa） Chain A 80–250（171 aa）	Mutation：YES Mutation：YES Mutation：YES	PO4 PHOSPHATE ION × 3	X-RAY DIFFRACTION X-ray crystallization conditions pH 8.2；1.75 M (NH4)2PO4, PH 8.2	Resolution 2.30 Å R-free 0.270
2V2H The A178L mutation in the C-terminal hinge of the flexible loop-6 of triosephosphate isomerase (TIM) induces a more closed conformation of this hinge region in dimeric and monomeric TIM Deposited 2007-06-06	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 1–13（13 aa） Chain A 15–72（58 aa） Chain A 80–250（171 aa） Chain B 1–13（13 aa） Chain B 15–72（58 aa） Chain B 80–250（171 aa） Chain C 1–13（13 aa） Chain C 15–72（58 aa） Chain C 80–250（171 aa）	Mutation：YES Mutation：YES Mutation：YES Mutation：YES Mutation：YES Mutation：YES Mutation：YES Mutation：YES Mutation：YES	PGA 2-PHOSPHOGLYCOLIC ACID × 3 CL CHLORIDE ION × 3	X-RAY DIFFRACTION X-ray crystallization conditions pH 5.5；0.1 M CITRIC ACID PH 5.5, 20% PEG 6K, 3% TERT.BUTANOL	Resolution 1.18 Å R-free 0.187
2V5L Structures of the Open and Closed State of Trypanosomal Triosephosphate Isomerase: as Observed in a New Crystal Form: Implications for the Reaction Mechanism Deposited 2007-07-06	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–250（250 aa）	Not recorded	SO4 SULFATE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 8.8；18% PEG6000, 200 MM TRIS PH 8.8, 1MM EDTA, 1MM DTT AND 1MM NAN3	Resolution 2.40 Å
2V5L Structures of the Open and Closed State of Trypanosomal Triosephosphate Isomerase: as Observed in a New Crystal Form: Implications for the Reaction Mechanism Deposited 2007-07-06	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain B 1–250（250 aa）	Not recorded	SO4 SULFATE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 8.8；18% PEG6000, 200 MM TRIS PH 8.8, 1MM EDTA, 1MM DTT AND 1MM NAN3	Resolution 2.40 Å
2VEI Structure-based enzyme engineering efforts with an inactive monomeric TIM variant: the importance of a single point mutation for generating an active site with suitable binding properties Deposited 2007-10-24	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 2–13（12 aa） Fragment：RESIDUES 2-13,15-72,80-234,238-250 Chain A 15–72（58 aa） Fragment：RESIDUES 2-13,15-72,80-234,238-250 Chain A 80–234（155 aa） Fragment：RESIDUES 2-13,15-72,80-234,238-250 Chain A 238–250（13 aa） Fragment：RESIDUES 2-13,15-72,80-234,238-250 Chain B 2–13（12 aa） Fragment：RESIDUES 2-13,15-72,80-234,238-250 Chain B 15–72（58 aa） Fragment：RESIDUES 2-13,15-72,80-234,238-250 Chain B 80–234（155 aa） Fragment：RESIDUES 2-13,15-72,80-234,238-250 Chain B 238–250（13 aa） Fragment：RESIDUES 2-13,15-72,80-234,238-250 Chain C 2–13（12 aa） Fragment：RESIDUES 2-13,15-72,80-234,238-250 Chain C 15–72（58 aa） Fragment：RESIDUES 2-13,15-72,80-234,238-250 Chain C 80–234（155 aa） Fragment：RESIDUES 2-13,15-72,80-234,238-250 Chain C 238–250（13 aa） Fragment：RESIDUES 2-13,15-72,80-234,238-250	Not recorded	SO4 SULFATE ION × 16	X-RAY DIFFRACTION X-ray crystallization conditions pH 8.5；0.1 M TRIS/HCL PH 8.5, 1.9 M MGSO4	Resolution 1.89 Å R-free 0.215
2VEK Structure-based enzyme engineering efforts with an inactive monomeric TIM variant: the importance of a single point mutation for generating an active site with suitable binding properties Deposited 2007-10-24	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 2–13（12 aa） Fragment：RESIDUES 2-13,15-72,80-234,238-250 Chain A 15–72（58 aa） Fragment：RESIDUES 2-13,15-72,80-234,238-250 Chain A 80–234（155 aa） Fragment：RESIDUES 2-13,15-72,80-234,238-250 Chain A 238–250（13 aa） Fragment：RESIDUES 2-13,15-72,80-234,238-250	Mutation：YES Mutation：YES Mutation：YES Mutation：YES	CIT CITRIC ACID × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 5.5；20% PEG6000, 2,5% T-BUTANOL, 0.1 M CITRIC ACID PH 5,5	Resolution 1.60 Å R-free 0.193
2VEK Structure-based enzyme engineering efforts with an inactive monomeric TIM variant: the importance of a single point mutation for generating an active site with suitable binding properties Deposited 2007-10-24	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 2–13（12 aa） Fragment：RESIDUES 2-13,15-72,80-234,238-250 Chain B 15–72（58 aa） Fragment：RESIDUES 2-13,15-72,80-234,238-250 Chain B 80–234（155 aa） Fragment：RESIDUES 2-13,15-72,80-234,238-250 Chain B 238–250（13 aa） Fragment：RESIDUES 2-13,15-72,80-234,238-250	Mutation：YES Mutation：YES Mutation：YES Mutation：YES	CIT CITRIC ACID × 1 TBU TERTIARY-BUTYL ALCOHOL × 1 ASF 3-(BUTYLSULPHONYL)-PROPANOIC ACID × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 5.5；20% PEG6000, 2,5% T-BUTANOL, 0.1 M CITRIC ACID PH 5,5	Resolution 1.60 Å R-free 0.193
2VEL Structure-based enzyme engineering efforts with an inactive monomeric TIM variant: the importance of a single point mutation for generating an active site with suitable binding properties. Deposited 2007-10-24	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 2–13（12 aa） Fragment：RESIDUES 2-13,15-72,80-234,238-250 Chain A 15–72（58 aa） Fragment：RESIDUES 2-13,15-72,80-234,238-250 Chain A 80–234（155 aa） Fragment：RESIDUES 2-13,15-72,80-234,238-250 Chain A 238–250（13 aa） Fragment：RESIDUES 2-13,15-72,80-234,238-250	Mutation：YES Mutation：YES Mutation：YES Mutation：YES	CL CHLORIDE ION × 1 PGA 2-PHOSPHOGLYCOLIC ACID × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 5.5；20% PEG6000, 2,5% T-BUTANOL, 0.1 M CITRIC ACID PH 5,5	Resolution 2.30 Å R-free 0.257
2VEL Structure-based enzyme engineering efforts with an inactive monomeric TIM variant: the importance of a single point mutation for generating an active site with suitable binding properties. Deposited 2007-10-24	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 2–13（12 aa） Fragment：RESIDUES 2-13,15-72,80-234,238-250 Chain B 15–72（58 aa） Fragment：RESIDUES 2-13,15-72,80-234,238-250 Chain B 80–234（155 aa） Fragment：RESIDUES 2-13,15-72,80-234,238-250 Chain B 238–250（13 aa） Fragment：RESIDUES 2-13,15-72,80-234,238-250	Mutation：YES Mutation：YES Mutation：YES Mutation：YES	CL CHLORIDE ION × 1 PGA 2-PHOSPHOGLYCOLIC ACID × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 5.5；20% PEG6000, 2,5% T-BUTANOL, 0.1 M CITRIC ACID PH 5,5	Resolution 2.30 Å R-free 0.257
2VEM Structure-based enzyme engineering efforts with an inactive monomeric TIM variant: the importance of a single point mutation for generating an active site with suitable binding properties Deposited 2007-10-25	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 2–13（12 aa） Fragment：RESIDUES 2-13,15-72,80-234,238-250 Chain A 15–72（58 aa） Fragment：RESIDUES 2-13,15-72,80-234,238-250 Chain A 80–234（155 aa） Fragment：RESIDUES 2-13,15-72,80-234,238-250 Chain A 238–250（13 aa） Fragment：RESIDUES 2-13,15-72,80-234,238-250	Mutation：YES Mutation：YES Mutation：YES Mutation：YES	BBR (3-bromo-2-oxo-propoxy)phosphonic acid × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 5.5；20% PEG6000, 2,5% T-BUTANOL, 0.1 M CITRIC ACID PH 5,5	Resolution 2.20 Å R-free 0.247
2VEM Structure-based enzyme engineering efforts with an inactive monomeric TIM variant: the importance of a single point mutation for generating an active site with suitable binding properties Deposited 2007-10-25	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 2–13（12 aa） Fragment：RESIDUES 2-13,15-72,80-234,238-250 Chain B 15–72（58 aa） Fragment：RESIDUES 2-13,15-72,80-234,238-250 Chain B 80–234（155 aa） Fragment：RESIDUES 2-13,15-72,80-234,238-250 Chain B 238–250（13 aa） Fragment：RESIDUES 2-13,15-72,80-234,238-250	Mutation：YES Mutation：YES Mutation：YES Mutation：YES	BBR (3-bromo-2-oxo-propoxy)phosphonic acid × 1 TBU TERTIARY-BUTYL ALCOHOL × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 5.5；20% PEG6000, 2,5% T-BUTANOL, 0.1 M CITRIC ACID PH 5,5	Resolution 2.20 Å R-free 0.247
2VEN Structure-based enzyme engineering efforts with an inactive monomeric TIM variant: the importance of a single point mutation for generating an active site with suitable binding properties Deposited 2007-10-25	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 2–250（249 aa） Fragment：RESIDUES 2-13,15-72,80-234,238-250	Mutation：YES	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 5.5；20% PEG6000, 2,5% T-BUTANOL, 0.1 M CITRIC ACID PH 5,5	Resolution 2.00 Å R-free 0.237
2VEN Structure-based enzyme engineering efforts with an inactive monomeric TIM variant: the importance of a single point mutation for generating an active site with suitable binding properties Deposited 2007-10-25	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 2–250（249 aa） Fragment：RESIDUES 2-13,15-72,80-234,238-250	Mutation：YES	CIT CITRIC ACID × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 5.5；20% PEG6000, 2,5% T-BUTANOL, 0.1 M CITRIC ACID PH 5,5	Resolution 2.00 Å R-free 0.237
2WSQ MonoTIM mutant RMM0-1, dimeric form. Deposited 2009-09-08	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain B 2–67（66 aa） Fragment：RESIDUES 2-67,84-250 Chain B 84–250（167 aa） Fragment：RESIDUES 2-67,84-250 Chain C 2–67（66 aa） Fragment：RESIDUES 2-67,84-250 Chain C 84–250（167 aa） Fragment：RESIDUES 2-67,84-250	Mutation：YES Mutation：YES Mutation：YES Mutation：YES	SO4 SULFATE ION × 5	X-RAY DIFFRACTION X-ray crystallization conditions pH 6.2；303 K；100 MM MES BUFFER PH 6.2, 180 MM LI2SO4, 26 PERCENT PEG 6000, 5 MM DITHIOTHREITOL, 1 MM EDTA AND 1 MM NAN3, AT 30 DEGREES CELSIUS.	Resolution 2.10 Å R-free 0.244
2WSQ MonoTIM mutant RMM0-1, dimeric form. Deposited 2009-09-08	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 2–67（66 aa） Fragment：RESIDUES 2-67,84-250 Chain A 84–250（167 aa） Fragment：RESIDUES 2-67,84-250 Chain D 2–67（66 aa） Fragment：RESIDUES 2-67,84-250 Chain D 84–250（167 aa） Fragment：RESIDUES 2-67,84-250	Mutation：YES Mutation：YES Mutation：YES Mutation：YES	SO4 SULFATE ION × 3	X-RAY DIFFRACTION X-ray crystallization conditions pH 6.2；303 K；100 MM MES BUFFER PH 6.2, 180 MM LI2SO4, 26 PERCENT PEG 6000, 5 MM DITHIOTHREITOL, 1 MM EDTA AND 1 MM NAN3, AT 30 DEGREES CELSIUS.	Resolution 2.10 Å R-free 0.244
2WSR MONOTIM MUTANT RMM0-1, MONOMERIC FORM. Deposited 2009-09-08	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 2–67（66 aa） Fragment：RESIDUES 2-67,84-250 Chain A 84–250（167 aa） Fragment：RESIDUES 2-67,84-250	Mutation：YES Mutation：YES	SO4 SULFATE ION × 4 AZI AZIDE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 6.2；291 K；100 MM MES BUFFER PH 6.2, 180 MM LI2SO4, 26 PERCENT PEG 6000, 5 MM DITHIOTHREITOL, 1 MM EDTA AND 1 MM NAN3, AT 18 DEGREES CELSIUS.	Resolution 1.65 Å R-free 0.255
2X16 Crystallographic binding studies with an engineered monomeric variant of triosephosphate isomerase Deposited 2009-12-21	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 2–13（12 aa） Fragment：RESIDUES 2-13,15-72,80-234,238-250 Chain A 15–72（58 aa） Fragment：RESIDUES 2-13,15-72,80-234,238-250 Chain A 80–234（155 aa） Fragment：RESIDUES 2-13,15-72,80-234,238-250 Chain A 238–250（13 aa） Fragment：RESIDUES 2-13,15-72,80-234,238-250	Mutation：YES Mutation：YES Mutation：YES Mutation：YES	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 5.5；20% PEG6000, 0.1M CITRATE PH 5.5	Resolution 2.13 Å R-free 0.261
2X16 Crystallographic binding studies with an engineered monomeric variant of triosephosphate isomerase Deposited 2009-12-21	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 2–13（12 aa） Fragment：RESIDUES 2-13,15-72,80-234,238-250 Chain B 15–72（58 aa） Fragment：RESIDUES 2-13,15-72,80-234,238-250 Chain B 80–234（155 aa） Fragment：RESIDUES 2-13,15-72,80-234,238-250 Chain B 238–250（13 aa） Fragment：RESIDUES 2-13,15-72,80-234,238-250	Mutation：YES Mutation：YES Mutation：YES Mutation：YES	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 5.5；20% PEG6000, 0.1M CITRATE PH 5.5	Resolution 2.13 Å R-free 0.261
2X1R Crystallographic binding studies with an engineered monomeric variant of triosephosphate isomerase Deposited 2010-01-04	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 2–13（12 aa） Fragment：RESIDUES 2-13,15-72,80-234,238-250 Chain A 15–72（58 aa） Fragment：RESIDUES 2-13,15-72,80-234,238-250 Chain A 80–234（155 aa） Fragment：RESIDUES 2-13,15-72,80-234,238-250 Chain A 238–250（13 aa） Fragment：RESIDUES 2-13,15-72,80-234,238-250	Mutation：YES Mutation：YES Mutation：YES Mutation：YES	SO4 SULFATE ION × 1 X1R 3-(PROPYLSULFONYL)PROPANOIC ACID × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 5.5；20% PEG6000, 0.1M CITRATE, PH 5.5	Resolution 1.98 Å R-free 0.226
2X1R Crystallographic binding studies with an engineered monomeric variant of triosephosphate isomerase Deposited 2010-01-04	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 2–13（12 aa） Fragment：RESIDUES 2-13,15-72,80-234,238-250 Chain B 15–72（58 aa） Fragment：RESIDUES 2-13,15-72,80-234,238-250 Chain B 80–234（155 aa） Fragment：RESIDUES 2-13,15-72,80-234,238-250 Chain B 238–250（13 aa） Fragment：RESIDUES 2-13,15-72,80-234,238-250	Mutation：YES Mutation：YES Mutation：YES Mutation：YES	SO4 SULFATE ION × 2 X1R 3-(PROPYLSULFONYL)PROPANOIC ACID × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 5.5；20% PEG6000, 0.1M CITRATE, PH 5.5	Resolution 1.98 Å R-free 0.226
2X1S Crystallographic binding studies with an engineered monomeric variant of triosephosphate isomerase Deposited 2010-01-04	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 2–13（12 aa） Fragment：RESIDUES 2-13,15-72,80-234,238-250 Chain A 15–72（58 aa） Fragment：RESIDUES 2-13,15-72,80-234,238-250 Chain A 80–234（155 aa） Fragment：RESIDUES 2-13,15-72,80-234,238-250 Chain A 238–250（13 aa） Fragment：RESIDUES 2-13,15-72,80-234,238-250	Mutation：YES Mutation：YES Mutation：YES Mutation：YES	X1S 3-SULFOPROPANOIC ACID × 1 SO4 SULFATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 5.5；20% PEG6000, 0.1M CITRATE, PH 5.5	Resolution 1.93 Å R-free 0.201
2X1S Crystallographic binding studies with an engineered monomeric variant of triosephosphate isomerase Deposited 2010-01-04	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 2–13（12 aa） Fragment：RESIDUES 2-13,15-72,80-234,238-250 Chain B 15–72（58 aa） Fragment：RESIDUES 2-13,15-72,80-234,238-250 Chain B 80–234（155 aa） Fragment：RESIDUES 2-13,15-72,80-234,238-250 Chain B 238–250（13 aa） Fragment：RESIDUES 2-13,15-72,80-234,238-250	Mutation：YES Mutation：YES Mutation：YES Mutation：YES	X1S 3-SULFOPROPANOIC ACID × 1 SO4 SULFATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 5.5；20% PEG6000, 0.1M CITRATE, PH 5.5	Resolution 1.93 Å R-free 0.201
2X1T Crystallographic binding studies with an engineered monomeric variant of triosephosphate isomerase Deposited 2010-01-04	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 2–13（12 aa） Fragment：RESIDUES 2-13,15-72,80-234,238-250 Chain A 15–72（58 aa） Fragment：RESIDUES 2-13,15-72,80-234,238-250 Chain A 80–234（155 aa） Fragment：RESIDUES 2-13,15-72,80-234,238-250 Chain A 238–250（13 aa） Fragment：RESIDUES 2-13,15-72,80-234,238-250	Mutation：YES Mutation：YES Mutation：YES Mutation：YES	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 5.5；20% PEG6000, 0.1M CITRATE, PH 5.5	Resolution 1.83 Å R-free 0.219
2X1T Crystallographic binding studies with an engineered monomeric variant of triosephosphate isomerase Deposited 2010-01-04	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 2–13（12 aa） Fragment：RESIDUES 2-13,15-72,80-234,238-250 Chain B 15–72（58 aa） Fragment：RESIDUES 2-13,15-72,80-234,238-250 Chain B 80–234（155 aa） Fragment：RESIDUES 2-13,15-72,80-234,238-250 Chain B 238–250（13 aa） Fragment：RESIDUES 2-13,15-72,80-234,238-250	Mutation：YES Mutation：YES Mutation：YES Mutation：YES	RES 4-PHOSPHO-D-ERYTHRONOHYDROXAMIC ACID × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 5.5；20% PEG6000, 0.1M CITRATE, PH 5.5	Resolution 1.83 Å R-free 0.219
2X1U Crystallographic binding studies with an engineered monomeric variant of triosephosphate isomerase Deposited 2010-01-04	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 2–13（12 aa） Fragment：RESIDUES 2-13,15-72,80-234,238-250 Chain A 15–72（58 aa） Fragment：RESIDUES 2-13,15-72,80-234,238-250 Chain A 80–234（155 aa） Fragment：RESIDUES 2-13,15-72,80-234,238-250 Chain A 238–250（13 aa） Fragment：RESIDUES 2-13,15-72,80-234,238-250	Mutation：YES Mutation：YES Mutation：YES Mutation：YES	SO4 SULFATE ION × 3	X-RAY DIFFRACTION X-ray crystallization conditions pH 5.5；20% PEG6000, 0.1M CITRATE, PH 5.5	Resolution 1.84 Å R-free 0.237
2X1U Crystallographic binding studies with an engineered monomeric variant of triosephosphate isomerase Deposited 2010-01-04	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 2–13（12 aa） Fragment：RESIDUES 2-13,15-72,80-234,238-250 Chain B 15–72（58 aa） Fragment：RESIDUES 2-13,15-72,80-234,238-250 Chain B 80–234（155 aa） Fragment：RESIDUES 2-13,15-72,80-234,238-250 Chain B 238–250（13 aa） Fragment：RESIDUES 2-13,15-72,80-234,238-250	Mutation：YES Mutation：YES Mutation：YES Mutation：YES	SO4 SULFATE ION × 3	X-RAY DIFFRACTION X-ray crystallization conditions pH 5.5；20% PEG6000, 0.1M CITRATE, PH 5.5	Resolution 1.84 Å R-free 0.237
2X2G CRYSTALLOGRAPHIC BINDING STUDIES WITH AN ENGINEERED MONOMERIC VARIANT OF TRIOSEPHOSPHATE ISOMERASE Deposited 2010-01-13	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 2–13（12 aa） Fragment：RESIDUES 2-13,15-72,80-234,238-250 Chain A 15–72（58 aa） Fragment：RESIDUES 2-13,15-72,80-234,238-250 Chain A 80–234（155 aa） Fragment：RESIDUES 2-13,15-72,80-234,238-250 Chain A 238–250（13 aa） Fragment：RESIDUES 2-13,15-72,80-234,238-250	Mutation：YES Mutation：YES Mutation：YES Mutation：YES	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 5.5；20% PEG6000, 0.1M CITRATE, PH 5.5	Resolution 1.90 Å R-free 0.224
2X2G CRYSTALLOGRAPHIC BINDING STUDIES WITH AN ENGINEERED MONOMERIC VARIANT OF TRIOSEPHOSPHATE ISOMERASE Deposited 2010-01-13	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 2–13（12 aa） Fragment：RESIDUES 2-13,15-72,80-234,238-250 Chain B 15–72（58 aa） Fragment：RESIDUES 2-13,15-72,80-234,238-250 Chain B 80–234（155 aa） Fragment：RESIDUES 2-13,15-72,80-234,238-250 Chain B 238–250（13 aa） Fragment：RESIDUES 2-13,15-72,80-234,238-250	Mutation：YES Mutation：YES Mutation：YES Mutation：YES	3PG 3-PHOSPHOGLYCERIC ACID × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 5.5；20% PEG6000, 0.1M CITRATE, PH 5.5	Resolution 1.90 Å R-free 0.224
2Y6Z Crystallographic structure of GM23 an example of Catalytic migration from TIM to thiamin phosphate synthase. Deposited 2011-01-27	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–250（250 aa）	Mutation：YES	TPS THIAMIN PHOSPHATE × 2 POP PYROPHOSPHATE 2- × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 6.5；PROTEIN WAS CRYSTALLIZED FROM 2 M LI2SO4, 100 MM MES, PH 6.5	Resolution 2.60 Å R-free 0.235
2Y70 CRYSTALLOGRAPHIC STRUCTURE OF GM23, MUTANT G89D, AN EXAMPLE OF CATALYTIC MIGRATION FROM TIM TO THIAMIN PHOSPHATE SYNTHASE. Deposited 2011-01-27	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain B 1–250（250 aa） Chain C 1–250（250 aa）	Mutation：YES Mutation：YES	SO4 SULFATE ION × 2 ACT ACETATE ION × 7	X-RAY DIFFRACTION X-ray crystallization conditions pH 6.5；PROTEIN WAS CRYSTALLIZED FROM 2M LI2SO4, 100 MM MES, PH 6.5	Resolution 2.30 Å R-free 0.230
2Y70 CRYSTALLOGRAPHIC STRUCTURE OF GM23, MUTANT G89D, AN EXAMPLE OF CATALYTIC MIGRATION FROM TIM TO THIAMIN PHOSPHATE SYNTHASE. Deposited 2011-01-27	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–250（250 aa） Chain D 1–250（250 aa）	Mutation：YES Mutation：YES	SO4 SULFATE ION × 2 ACT ACETATE ION × 10	X-RAY DIFFRACTION X-ray crystallization conditions pH 6.5；PROTEIN WAS CRYSTALLIZED FROM 2M LI2SO4, 100 MM MES, PH 6.5	Resolution 2.30 Å R-free 0.230
3Q37 Identification of Amino Acids that Account for Long-Range Interactions in Proteins Using Two Triosephosphate Isomerases from Pathogenic Trypanosomes. Deposited 2010-12-21	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 2–35（34 aa） Fragment：UNP P04789 residues 2-35 and 92-119, UNP P52270 residues 35-92 and 121-251 Chain A 92–119（28 aa） Fragment：UNP P04789 residues 2-35 and 92-119, UNP P52270 residues 35-92 and 121-251 Chain B 2–35（34 aa） Fragment：UNP P04789 residues 2-35 and 92-119, UNP P52270 residues 35-92 and 121-251 Chain B 92–119（28 aa） Fragment：UNP P04789 residues 2-35 and 92-119, UNP P52270 residues 35-92 and 121-251	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7；278 K；0.2 Sodium malonate, 20% PEG 3350, pH 7.0, VAPOR DIFFUSION, SITTING DROP, temperature 278K	Resolution 1.65 Å R-free 0.220
3Q37 Identification of Amino Acids that Account for Long-Range Interactions in Proteins Using Two Triosephosphate Isomerases from Pathogenic Trypanosomes. Deposited 2010-12-21	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 2 Insufficient information Homooligomer；Protein × 2 PDB declaration: dimeric	Chain C 2–35（34 aa） Fragment：UNP P04789 residues 2-35 and 92-119, UNP P52270 residues 35-92 and 121-251 Chain C 92–119（28 aa） Fragment：UNP P04789 residues 2-35 and 92-119, UNP P52270 residues 35-92 and 121-251 Chain D 2–35（34 aa） Fragment：UNP P04789 residues 2-35 and 92-119, UNP P52270 residues 35-92 and 121-251 Chain D 92–119（28 aa） Fragment：UNP P04789 residues 2-35 and 92-119, UNP P52270 residues 35-92 and 121-251	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7；278 K；0.2 Sodium malonate, 20% PEG 3350, pH 7.0, VAPOR DIFFUSION, SITTING DROP, temperature 278K	Resolution 1.65 Å R-free 0.220
3TIM THE CRYSTAL STRUCTURE OF THE "OPEN" AND THE "CLOSED" CONFORMATION OF THE FLEXIBLE LOOP OF TRYPANOSOMAL TRIOSEPHOSPHATE ISOMERASE Deposited 1990-05-15	Different construct Different mutation/modification Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–250（250 aa） Chain B 1–250（250 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.80 Å
4JEQ Different Contribution of Conserved Amino Acids to the Global Properties of Homologous Enzymes Deposited 2013-02-27	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–250（250 aa） Chain B 1–250（250 aa）	Mutation：E104D Mutation：E104D	SO4 SULFATE ION × 1 PEG DI(HYDROXYETHYL)ETHER × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.6；281.15 K；25% w/v PEG monomethyl ether 2000, 0.1 M Tris, 0.01 M Nickel (II) chloride hexahydrate, 5% w/v n-dodecyl-N,N-dimethylamin-N-oxide , pH 8.6, VAPOR DIFFUSION, SITTING DROP, temperature 281.15K	Resolution 2.30 Å R-free 0.261
4JEQ Different Contribution of Conserved Amino Acids to the Global Properties of Homologous Enzymes Deposited 2013-02-27	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain C 1–250（250 aa） Chain D 1–250（250 aa）	Mutation：E104D Mutation：E104D	SO4 SULFATE ION × 2 PEG DI(HYDROXYETHYL)ETHER × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.6；281.15 K；25% w/v PEG monomethyl ether 2000, 0.1 M Tris, 0.01 M Nickel (II) chloride hexahydrate, 5% w/v n-dodecyl-N,N-dimethylamin-N-oxide , pH 8.6, VAPOR DIFFUSION, SITTING DROP, temperature 281.15K	Resolution 2.30 Å R-free 0.261
4JEQ Different Contribution of Conserved Amino Acids to the Global Properties of Homologous Enzymes Deposited 2013-02-27	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain E 1–250（250 aa） Chain F 1–250（250 aa）	Mutation：E104D Mutation：E104D	PEG DI(HYDROXYETHYL)ETHER × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.6；281.15 K；25% w/v PEG monomethyl ether 2000, 0.1 M Tris, 0.01 M Nickel (II) chloride hexahydrate, 5% w/v n-dodecyl-N,N-dimethylamin-N-oxide , pH 8.6, VAPOR DIFFUSION, SITTING DROP, temperature 281.15K	Resolution 2.30 Å R-free 0.261
4JEQ Different Contribution of Conserved Amino Acids to the Global Properties of Homologous Enzymes Deposited 2013-02-27	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 4 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain G 1–250（250 aa） Chain H 1–250（250 aa）	Mutation：E104D Mutation：E104D	SO4 SULFATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.6；281.15 K；25% w/v PEG monomethyl ether 2000, 0.1 M Tris, 0.01 M Nickel (II) chloride hexahydrate, 5% w/v n-dodecyl-N,N-dimethylamin-N-oxide , pH 8.6, VAPOR DIFFUSION, SITTING DROP, temperature 281.15K	Resolution 2.30 Å R-free 0.261
4JEQ Different Contribution of Conserved Amino Acids to the Global Properties of Homologous Enzymes Deposited 2013-02-27	Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 5 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain I 1–250（250 aa） Chain J 1–250（250 aa）	Mutation：E104D Mutation：E104D	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.6；281.15 K；25% w/v PEG monomethyl ether 2000, 0.1 M Tris, 0.01 M Nickel (II) chloride hexahydrate, 5% w/v n-dodecyl-N,N-dimethylamin-N-oxide , pH 8.6, VAPOR DIFFUSION, SITTING DROP, temperature 281.15K	Resolution 2.30 Å R-free 0.261
4JEQ Different Contribution of Conserved Amino Acids to the Global Properties of Homologous Enzymes Deposited 2013-02-27	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 6 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain K 1–250（250 aa） Chain L 1–250（250 aa）	Mutation：E104D Mutation：E104D	SO4 SULFATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.6；281.15 K；25% w/v PEG monomethyl ether 2000, 0.1 M Tris, 0.01 M Nickel (II) chloride hexahydrate, 5% w/v n-dodecyl-N,N-dimethylamin-N-oxide , pH 8.6, VAPOR DIFFUSION, SITTING DROP, temperature 281.15K	Resolution 2.30 Å R-free 0.261
4TIM CRYSTALLOGRAPHIC AND MOLECULAR MODELING STUDIES ON TRYPANOSOMAL TRIOSEPHOSPHATE ISOMERASE: A CRITICAL ASSESSMENT OF THE PREDICTED AND OBSERVED STRUCTURES OF THE COMPLEX WITH 2-PHOSPHOGLYCERATE Deposited 1991-04-11	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–250（250 aa） Chain B 1–250（250 aa）	Not recorded	2PG 2-PHOSPHOGLYCERIC ACID × 1	X-RAY DIFFRACTION X-ray crystallization conditions THE CRYSTALS USED FOR THIS STRUCTURE DETERMINATION WERE GROWN IN THE PRESENCE OF 2.4M AMMONIUM SULFATE (SEE PROTEIN DATA BANK ENTRIES 2TIM AND 5TIM), BUT BEFORE DATA COLLECTION THESE CRYSTALS WERE TRANSFERRED TO A MOTHER LIQUOR WITHOUT SULFATE CONTAINING 30MM 2-PHOSPHOGLYCERATE. THE ACTIVE SITE OF CHAIN A ("OPEN"-CONFORMATION) HAS NO BOUND 2-PHOSPHOGLYCERATE. THE ACTIVE SITE OF CHAIN B ("CLOSED"-CONFORMATION) HAS A BOUND 2-PHOSPHOGLYCERATE.	Resolution 2.40 Å
5I3F Structure-Function Studies on Role of Hydrophobic Clamping of a Basic Glutamate in Catalysis by Triosephosphate Isomerase Deposited 2016-02-10	Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–250（250 aa） Chain B 1–250（250 aa）	Mutation：I172A Mutation：I172A	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6；287 K；20-30% MePEG 5000, 50 mM MES	Resolution 1.72 Å R-free 0.227
5I3F Structure-Function Studies on Role of Hydrophobic Clamping of a Basic Glutamate in Catalysis by Triosephosphate Isomerase Deposited 2016-02-10	Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain C 1–250（250 aa） Chain D 1–250（250 aa）	Mutation：I172A Mutation：I172A	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6；287 K；20-30% MePEG 5000, 50 mM MES	Resolution 1.72 Å R-free 0.227
5I3G Structure-Function Studies on Role of Hydrophobic Clamping of a Basic Glutamate in Catalysis by Triosephosphate Isomerase Deposited 2016-02-10	Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–250（250 aa） Chain C 1–250（250 aa）	Mutation：I172A,L232A Mutation：I172A,L232A	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；287 K；15-25% Peg 8000, 50-100 mM potassium acetate, 100 mM BTP pH 7.0	Resolution 1.96 Å R-free 0.222
5I3G Structure-Function Studies on Role of Hydrophobic Clamping of a Basic Glutamate in Catalysis by Triosephosphate Isomerase Deposited 2016-02-10	Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain B 1–250（250 aa） Chain D 1–250（250 aa）	Mutation：I172A,L232A Mutation：I172A,L232A	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；287 K；15-25% Peg 8000, 50-100 mM potassium acetate, 100 mM BTP pH 7.0	Resolution 1.96 Å R-free 0.222
5I3H Structure-Function Studies on Role of Hydrophobic Clamping of a Basic Glutamate in Catalysis by Triosephosphate Isomerase Deposited 2016-02-10	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–250（250 aa） Chain B 1–250（250 aa）	Mutation：I172A, L232A Mutation：I172A, L232A	K POTASSIUM ION × 2 PGA 2-PHOSPHOGLYCOLIC ACID × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；287 K；15-25% Peg 8000, 50-100 mM potassium acetate, 100 mM BTP pH 7.0	Resolution 2.25 Å R-free 0.211
5I3I Structure-Function Studies on Role of Hydrophobic Clamping of a Basic Glutamate in Catalysis by Triosephosphate Isomerase Deposited 2016-02-10	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–250（250 aa） Chain B 1–250（250 aa）	Mutation：I172A Mutation：I172A	PGA 2-PHOSPHOGLYCOLIC ACID × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6；287 K；20-30% MePEG 5000, 2-4% PEP, 50 mM MES	Resolution 2.20 Å R-free 0.249
5I3I Structure-Function Studies on Role of Hydrophobic Clamping of a Basic Glutamate in Catalysis by Triosephosphate Isomerase Deposited 2016-02-10	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain C 1–250（250 aa） Chain D 1–250（250 aa）	Mutation：I172A Mutation：I172A	PGA 2-PHOSPHOGLYCOLIC ACID × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6；287 K；20-30% MePEG 5000, 2-4% PEP, 50 mM MES	Resolution 2.20 Å R-free 0.249
5I3J Structure-Function Studies on Role of Hydrophobic Clamping of a Basic Glutamate in Catalysis by Triosephosphate Isomerase Deposited 2016-02-10	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–250（250 aa） Chain B 1–250（250 aa）	Mutation：L232A Mutation：L232A	NA SODIUM ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；287 K；20-30% Peg 4000, 150-250 mM NaCl, 50 mM Epps	Resolution 1.80 Å R-free 0.211
5I3K Structure-Function Studies on Role of Hydrophobic Clamping of a Basic Glutamate in Catalysis by Triosephosphate Isomerase Deposited 2016-02-10	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–250（250 aa） Chain D 1–250（250 aa）	Mutation：L232A Mutation：L232A	NA SODIUM ION × 2 PGA 2-PHOSPHOGLYCOLIC ACID × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；287 K；20-30% Peg 4000, 150-250 mM NaCl, 50 mM Epps	Resolution 2.21 Å R-free 0.264
5I3K Structure-Function Studies on Role of Hydrophobic Clamping of a Basic Glutamate in Catalysis by Triosephosphate Isomerase Deposited 2016-02-10	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain B 1–250（250 aa） Chain C 1–250（250 aa）	Mutation：L232A Mutation：L232A	NA SODIUM ION × 1 PGA 2-PHOSPHOGLYCOLIC ACID × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；287 K；20-30% Peg 4000, 150-250 mM NaCl, 50 mM Epps	Resolution 2.21 Å R-free 0.264
5TIM REFINED 1.83 ANGSTROMS STRUCTURE OF TRYPANOSOMAL TRIOSEPHOSPHATE ISOMERASE, CRYSTALLIZED IN THE PRESENCE OF 2.4 M-AMMONIUM SULPHATE. A COMPARISON WITH THE STRUCTURE OF THE TRYPANOSOMAL TRIOSEPHOSPHATE ISOMERASE-GLYCEROL-3-PHOSPHATE COMPLEX Deposited 1991-04-23	Different construct Different mutation/modification Different ligand/ion Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–250（250 aa） Chain B 1–250（250 aa）	Not recorded	SO4 SULFATE ION × 2 DTT 2,3-DIHYDROXY-1,4-DITHIOBUTANE × 1	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 1.83 Å
6TIM THE ADAPTABILITY OF THE ACTIVE SITE OF TRYPANOSOMAL TRIOSEPHOSPHATE ISOMERASE AS OBSERVED IN THE CRYSTAL STRUCTURES OF THREE DIFFERENT COMPLEXES Deposited 1991-04-23	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–250（250 aa） Chain B 1–250（250 aa）	Not recorded	G3P SN-GLYCEROL-3-PHOSPHATE × 1	X-RAY DIFFRACTION X-ray crystallization conditions THIS STRUCTURE IS OBTAINED FROM CRYSTALS GROWN IN 2.4M AMMONIUM SULPHATE AND TRANSFERRED INTO SULPHATE FREE MOTHER LIQUOR CONTAINING 6MM DL-GLYCEROL-3-PHOSPHATE.	Resolution 2.20 Å

48 other PDB entries and 80 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	TPIS_TRYBB
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–250； UniProt 1–250

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

Download Download SAXS (.dat) P(r) (.pr.out) CIF

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	1tpe
Deposition date deposition_date	1994-02-28
Structure title title	COMPARISON OF THE STRUCTURES AND THE CRYSTAL CONTACTS OF TRYPANOSOMAL TRIOSEPHOSPHATE ISOMERASE IN FOUR DIFFERENT CRYSTAL FORMS
Keywords keywords	ISOMERASE(INTRAMOLECULAR OXIDOREDUCTASE); ISOMERASE(INTRAMOLECULAR OXIDOREDUCTASE)
Experimental Method method	X-RAY DIFFRACTION

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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier	18.55 Å
Radius of gyration Rg (electron density) rg_electron	17.28 Å
Forward intensity I(0) i0	12429600.00
Molecular weight molecular_weight	26795.0 kDa
Excluded volume excluded_volume	33815 Å³
Envelope volume envelope_volume	38429 Å³
Hydration-shell volume shell_volume	18344 Å³
Envelope diameter envelope_diameter	55.0 Å
Shell Rg shell_rg	23.67 Å
Envelope Rg envelope_rg	17.48 Å
Shape Rg shape_rg	17.26 Å
Total Rg total_rg	18.34 Å
Total atoms total_atoms	1889
Residues n_residues	249
Spherical-harmonic order n_harmonics	20
q range q_range	— – 0.5000 Å⁻¹
Data points n_points	101
Shell type shell_type	directional
Solvent electron density solvent_density	0.3340 e/Å³
Shell contrast contrast_shell	0.0300 e/Å³
CRYSOL version crysol_version	4.1.3

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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax	55.2 Å
Rg (real space) rg_real	18.42 Å
Rg uncertainty (real space) rg_real_error	0.26 Å
I(0) (real space) i0_real	1.2430e+07
I(0) uncertainty (real space) i0_real_error	1.5260e+05
Rg (reciprocal space) rg_reciprocal	18.44 Å
I(0) (reciprocal space) i0_reciprocal	12430000.0000
Solution quality estimate total_estimate	0.8924
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	1
Primary peak position r_peak_primary	54.5 Å
Skewness Skewness skewness	0.081
Kurtosis Kurtosis kurtosis	-0.484
Angular range angular_range	— – 0.4300 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	2871000.0000
Real-space data points n_real_points	74
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.942; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.977; Smooth: 0.797

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (2)

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7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_id	d1tpea_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.1 — TIM beta/alpha-barrel
Superfamily Superfamily superfamily	c.1.1 — Triosephosphate isomerase (TIM)
Family Family family	c.1.1.1 — Triosephosphate isomerase (TIM)

CATH v4.4 (1 domains)

Domain ID domain_id	1tpeA00
Class class	3 — Alpha Beta
Architecture architecture	20 — Alpha-Beta Barrel
Topology topology	20 — TIM Barrel
Homologous superfamily homologous superfamily	70 — Aldolase class I

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8. Citations (1)

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Unit-cell length a length_a	95.400 Å
Unit-cell length b length_b	48.200 Å
Unit-cell length c length_c	67.500 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	120.00 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	4

Space group space_group	C 1 2 1
Space-group number int_tables_number	5
Crystal system crystal_system	—

Resolution resolution	2.100 Å
Low-resolution limit resolution_low	15.000 Å
R factor r_factor	0.1550
R_work r_work	0.1550
R_free r_free	—

Description description	TRIOSEPHOSPHATE ISOMERASE
Molecular weight formula_weight	26951.9 kDa
EC 编号 ec_number	5.3.1.1
Source method src_method	man
Copy count entity_count	1

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	1989

COMPARISON OF THE STRUCTURES AND THE CRYSTAL CONTACTS OF TRYPANOSOMAL TRIOSEPHOSPHATE ISOMERASE IN FOUR DIFFERENT CRYSTAL FORMS

1. Protein Identity and Related Structures Protein Identity & Related Structures

TRIOSEPHOSPHATE ISOMERASE

State in the Current Structure

Other States of the Same Protein in the Database

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

2. Structure Basics 2. Structure Basics

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

5. Crystallography and Experiment 5. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

6. Entities and Polymers Entities & Polymers (2)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 water

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

CATH v4.4 (1 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)

来源生物 organism	Trypanosoma brucei brucei
NCBI Class编号 ncbi_taxonomy_id	5702

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	100

fit	/app/data/saxs_computation/tp/1tpe/1tpe.fit
pddf	/app/data/pr_computation/tp/1tpe/1tpe.pr.out
profile	/app/data/saxs_computation/tp/1tpe/1tpe.dat