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Yorodumi- PDB-1tti: THREE NEW CRYSTAL STRUCTURES OF POINT MUTATION VARIANTS OF MONOTI... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1tti | ||||||
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Title | THREE NEW CRYSTAL STRUCTURES OF POINT MUTATION VARIANTS OF MONOTIM: CONFORMATIONAL FLEXIBILITY OF LOOP-1,LOOP-4 AND LOOP-8 | ||||||
Components | TRIOSEPHOSPHATE ISOMERASE | ||||||
Keywords | ISOMERASE(INTRAMOLECULAR OXIDOREDUCTASE) | ||||||
Function / homology | Function and homology information glycosome / triose-phosphate isomerase / triose-phosphate isomerase activity / gluconeogenesis / glycolytic process / cytoplasm Similarity search - Function | ||||||
Biological species | Trypanosoma brucei brucei (eukaryote) | ||||||
Method | X-RAY DIFFRACTION / Resolution: 2.4 Å | ||||||
Authors | Radha Kishan, K.V. / Wierenga, R.K. | ||||||
Citation | Journal: Structure / Year: 1995 Title: Three new crystal structures of point mutation variants of monoTIM: conformational flexibility of loop-1, loop-4 and loop-8. Authors: Borchert, T.V. / Kishan, K.V. / Zeelen, J.P. / Schliebs, W. / Thanki, N. / Abagyan, R. / Jaenicke, R. / Wierenga, R.K. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1tti.cif.gz | 57.5 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1tti.ent.gz | 41.8 KB | Display | PDB format |
PDBx/mmJSON format | 1tti.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/tt/1tti ftp://data.pdbj.org/pub/pdb/validation_reports/tt/1tti | HTTPS FTP |
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-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 26193.943 Da / Num. of mol.: 1 / Mutation: I68G, A69N, K70A, S71D, DEL(73-79), P81A, A100W Source method: isolated from a genetically manipulated source Details: MONOTIM WITH A110W MUTATION / Source: (gene. exp.) Trypanosoma brucei brucei (eukaryote) / Species: Trypanosoma brucei / Strain: brucei Description: ESCHERICHIA COLI STRAIN XL1-BLUE USED FOR THE GENETIC MANIPULATIONS Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) / References: UniProt: P04789, triose-phosphate isomerase |
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#2: Chemical | ChemComp-PGA / |
#3: Water | ChemComp-HOH / |
Nonpolymer details | THERE IS ONE MOLECULE PER ASYMMETRIC UNIT. THERE IS ONE SUBSTRATE ANALOGUE, BOUND IN THE ACTIVE ...THERE IS ONE MOLECULE PER ASYMMETRIC |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 2.26 Å3/Da / Density % sol: 45.59 % | ||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | *PLUS Temperature: 20 R.T. / pH: 6.5 / Method: vapor diffusion, hanging drop | ||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Reflection | Resolution: 2.4→32 Å / Num. obs: 7034 / % possible obs: 25 % / Observed criterion σ(I): 0 |
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Reflection | *PLUS % possible obs: 75 % / Num. measured all: 11293 / Rmerge(I) obs: 0.065 |
Reflection shell | *PLUS Highest resolution: 2.4 Å / Lowest resolution: 2.6 Å / % possible obs: 25 % |
-Processing
Software |
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Refinement | Resolution: 2.4→32 Å / σ(F): 0
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Refinement step | Cycle: LAST / Resolution: 2.4→32 Å
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Refine LS restraints |
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Refinement | *PLUS Rfactor obs: 0.178 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS Type: x_angle_deg / Dev ideal: 2.3 |