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Yorodumi- PDB-1mss: LARGE SCALE STRUCTURAL REARRANGEMENTS OF THE FRONT LOOPS IN MONOM... -
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-Basic information
Entry | Database: PDB / ID: 1mss | ||||||
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Title | 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 | ||||||
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. #1: Journal: Structure / Year: 1993 Title: The Crystal Structure of an Engineered Monomeric Triose Phosphate Isomerase, Monotim: The Correct Modelling of an Eight-Residue Loop Authors: Borchert, T.V. / Abagyan, R. / Radha Kishan, K.V. / Zeelen, J.P. / 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 | 1mss.cif.gz | 101.5 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1mss.ent.gz | 78.2 KB | Display | PDB format |
PDBx/mmJSON format | 1mss.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ms/1mss ftp://data.pdbj.org/pub/pdb/validation_reports/ms/1mss | 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: 26020.688 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Trypanosoma brucei brucei (eukaryote) / Species: Trypanosoma brucei / Strain: brucei / References: UniProt: P04789, triose-phosphate isomerase #2: Water | ChemComp-HOH / | Sequence details | THERE ARE NO BREAKS IN THE PROTEIN CHAIN FOR EITHER OF THE MOLECULES BUT THERE IS A BREAK IN THE ...THERE ARE NO BREAKS IN THE PROTEIN CHAIN FOR EITHER OF THE MOLECULES BUT THERE IS A BREAK IN THE NUMBERING OF THE CHAINS. THIS IS DUE TO A LOOP DELETION MUTATION. RESIDUES 72 AND 80 ARE CONNECTED BY A PEPTIDE BOND. THERE IS ONE BREAK IN THE SEQUENCE AT 73. RESIDUE NUMBERS 73 - 79 ARE MISSING DUE TO DELETION OF A LOOP FROM THE PARENT MODEL AND CONNECTING | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 2.49 Å3/Da / Density % sol: 50.54 % | ||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | *PLUS pH: 8.5 / Method: vapor diffusion, hanging drop | ||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Radiation | Scattering type: x-ray |
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Radiation wavelength | Relative weight: 1 |
Reflection | *PLUS Highest resolution: 2.4 Å / Num. obs: 13847 / % possible obs: 71 % / Num. measured all: 22787 / Rmerge(I) obs: 0.044 |
Reflection shell | *PLUS Highest resolution: 2.4 Å / Lowest resolution: 2.6 Å / % possible obs: 20 % |
-Processing
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Refinement | Resolution: 2.4→24 Å /
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Refinement step | Cycle: LAST / Resolution: 2.4→24 Å
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Refine LS restraints |
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