Current Protein Identity：P04789
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Difference tags compare only the current result set; every original PDB and assembly record remains separate.
Related-Structure Differences
Each row represents one biological assembly in one PDB entry; multiple monomers of the same protein are listed separately.
| PDB Entry | Assembly / Oligomeric State | Construct | Mutations and Modifications | Ligands, Ions and Non-polymers | Experimental Method | Experimental Conditions | Structure Quality |
|---|---|---|---|---|---|---|---|
| 1AG1 MONOHYDROGEN PHOSPHATE BINDING TO TRYPANOSOMAL TRIOSEPHOSPHATE ISOMERASE Deposited 1997-03-28 | Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count |
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 | Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count |
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 | Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count |
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 | Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count |
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 | Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count |
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 | Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count |
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 | Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count |
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 | Assembly 3 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count |
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 | Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count |
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 | Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count |
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 | Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count |
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 | Assembly 3 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count |
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 |
| 1TPE COMPARISON OF THE STRUCTURES AND THE CRYSTAL CONTACTS OF TRYPANOSOMAL TRIOSEPHOSPHATE ISOMERASE IN FOUR DIFFERENT CRYSTAL FORMS Deposited 1994-02-28 | Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count |
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 |
| 1TPF COMPARISON OF THE STRUCTURES AND THE CRYSTAL CONTACTS OF TRYPANOSOMAL TRIOSEPHOSPHATE ISOMERASE IN FOUR DIFFERENT CRYSTAL FORMS Deposited 1994-02-28 | Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count |
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 | Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count |
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 | Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count |
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 | Assembly 3 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count |
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 | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count |
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 | Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count |
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 | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count |
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 | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count |
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 | Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count |
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 | Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count |
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 | Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count |
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 | Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count |
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 | Assembly 3 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count |
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 | Assembly 4 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count |
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 | Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count |
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 | Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric（3） Consistent with protein count |
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 | Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric（3） Consistent with protein count |
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 | Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count |
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 | Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count |
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 | Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric（3） Consistent with protein count |
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 | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count |
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 | Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count |
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 | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count |
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 | Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count |
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 | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count |
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 | Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count |
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 | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count |
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 | Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count |
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 | Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count |
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 | Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count |
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 | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count |
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 | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count |
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 | Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count |
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 | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count |
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 | Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count |
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 | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count |
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 | Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count |
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 | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count |
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 | Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count |
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 | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count |
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 | Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count |
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 | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count |
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 | Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count |
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 | Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count |
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 | Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count |
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 | Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count |
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 | Assembly 1 Insufficient information Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count |
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 | Assembly 2 Insufficient information Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count |
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 | Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count |
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 | Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count |
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 | Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count |
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 | Assembly 3 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count |
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 | Assembly 4 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count |
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 | Assembly 5 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count |
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 | Assembly 6 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count |
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 | Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count |
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 | Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count |
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 | Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count |
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 | Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count |
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 | Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count |
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 | Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count |
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 | Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count |
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 | Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count |
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 | Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count |
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 | Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count |
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 | Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count |
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 | Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count |
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 | Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count |
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 |