+Open data
-Basic information
Entry | Database: PDB / ID: 1tpc | ||||||
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Title | OFFSET OF A CATALYTIC LESION BY A BOUND WATER SOLUBLE | ||||||
Components | TRIOSEPHOSPHATE ISOMERASE | ||||||
Keywords | ISOMERASE(INTRAMOLECULAR OXIDOREDUCTASE) | ||||||
Function / homology | Function and homology information Glycolysis / Glycolysis / Gluconeogenesis / Gluconeogenesis / methylglyoxal biosynthetic process / methylglyoxal synthase / methylglyoxal synthase activity / glyceraldehyde-3-phosphate biosynthetic process / glycerol catabolic process / triose-phosphate isomerase ...Glycolysis / Glycolysis / Gluconeogenesis / Gluconeogenesis / methylglyoxal biosynthetic process / methylglyoxal synthase / methylglyoxal synthase activity / glyceraldehyde-3-phosphate biosynthetic process / glycerol catabolic process / triose-phosphate isomerase / triose-phosphate isomerase activity / canonical glycolysis / gluconeogenesis / glycolytic process / ubiquitin protein ligase binding / protein homodimerization activity / cytosol Similarity search - Function | ||||||
Biological species | Gallus gallus (chicken) | ||||||
Method | X-RAY DIFFRACTION / Resolution: 1.9 Å | ||||||
Authors | Zhang, Z. / Sugio, S. / Komives, E.A. / Liu, K.D. / Knowles, J.R. / Petsko, G.A. / Ringe, D. | ||||||
Citation | Journal: Biochemistry / Year: 1995 Title: The structural basis for pseudoreversion of the E165D lesion by the secondary S96P mutation in triosephosphate isomerase depends on the positions of active site water molecules. Authors: Komives, E.A. / Lougheed, J.C. / Liu, K. / Sugio, S. / Zhang, Z. / Petsko, G.A. / Ringe, D. #1: Journal: To be Published Title: Offset of a Catalytic Lesion (Glu165Asp) of Triosephosphate Isomerase by Bound Waters Soluble Authors: Zhang, Z. / Komives, E.A. / Sugio, S. / Liu, K.D. / Knowles, J.R. / Petsko, G.A. / Ringe, D. #2: Journal: To be Published Title: Triosephosphate Isomerase Drinks Water to Keep Healthy Authors: Zhang, Z. / Sugio, S. / Stock, A.M. / Komives, E.A. / Liu, K.D. / Narayana, N. / Huong, Ng.H. / Knowles, J.R. / Petsko, G.A. / Ringe, D. #3: Journal: To be Published Title: The Structural Basis for Pseudoreversion of the E165D Lesion by the Secondary S96P Mutation in Triosephosphate Isomerase Depends on the Position of Bound Water Molecules Authors: Komives, E.A. / Lougheed, J.C. / Zhang, Z. / Petsko, G.A. / Ringe, D. #4: Journal: To be Published Title: S96P Change is the Second-Site Suppressor for the H95N Sluggish Mutant Isomerase Authors: Zhang, Z. / Sugio, S. / Komives, E.A. / Liu, K.D. / Stock, A.M. / Narayana, N. / Xuong, Ng.H. / Knowles, J.R. / Petsko, G.A. / Ringe, D. #5: Journal: Biochemistry / Year: 1990 Title: How Can a Catalytic Lesion be Offset? the Energetics of Two Pseudorevertant Triosephosphate Isomerases Authors: Blacklow, S.C. / Knowles, J.R. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1tpc.cif.gz | 107 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1tpc.ent.gz | 82.8 KB | Display | PDB format |
PDBx/mmJSON format | 1tpc.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/tp/1tpc ftp://data.pdbj.org/pub/pdb/validation_reports/tp/1tpc | 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: 26536.301 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Gallus gallus (chicken) / References: UniProt: P00940, triose-phosphate isomerase #2: Chemical | #3: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 2.65 Å3/Da / Density % sol: 53.64 % | ||||||||||||||||||||||||||||||||||||
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Crystal grow | *PLUS Method: vapor diffusion, hanging drop | ||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Reflection | *PLUS Highest resolution: 1.9 Å / Lowest resolution: 50 Å / Num. obs: 37566 / % possible obs: 83 % / Num. measured all: 107422 / Rmerge(I) obs: 0.085 |
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-Processing
Software | Name: PROLSQ / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Refinement | Resolution: 1.9→6 Å / σ(F): 1 /
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Refinement step | Cycle: LAST / Resolution: 1.9→6 Å
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Refine LS restraints |
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Refinement | *PLUS Highest resolution: 2 Å / Num. reflection obs: 28952 / Rfactor obs: 0.174 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS |