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Open data
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Basic information
Entry | Database: PDB / ID: 6fit | ||||||
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Title | FHIT-TRANSITION STATE ANALOG | ||||||
![]() | FRAGILE HISTIDINE TRIAD PROTEIN![]() | ||||||
![]() | ![]() ![]() ![]() ![]() ![]() | ||||||
Function / homology | ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Lima, C.D. / Klein, M.G. / Hendrickson, W.A. | ||||||
![]() | ![]() Title: Structure-based analysis of catalysis and substrate definition in the HIT protein family. Authors: Lima, C.D. / Klein, M.G. / Hendrickson, W.A. #1: ![]() Title: MAD Analysis of Fhit, a Putative Human Tumor Suppressor from the Hit Protein Family Authors: Lima, C.D. / D'Amico, K.L. / Naday, I. / Rosenbaum, G. / Westbrook, E.M. / Hendrickson, W.A. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 39.9 KB | Display | ![]() |
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PDB format | ![]() | 27.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
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Links
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Assembly
Deposited unit | ![]()
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1 | ![]()
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Unit cell |
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Components
#1: Protein | ![]() Mass: 16886.203 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Description: EXPRESSED AS FUSION PROTEIN WITH GLUTATHIONE-S-TRANSFERASE IN ESCHERICHIA COLI Gene: FHIT / Plasmid: PGEX-2T / Gene (production host): FHIT / Production host: ![]() ![]() ![]() References: UniProt: P49789, ![]() |
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#2: Chemical | ChemComp-AMW / |
#3: Water | ChemComp-HOH / ![]() |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.93 Å3/Da / Density % sol: 58.04 % | ||||||||||||||||||||
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Crystal grow![]() | pH: 6.5 / Details: GROWN FROM AMMONIUM SULFATE, PH 6.5 | ||||||||||||||||||||
Crystal grow | *PLUS Method: unknown / Details: Lima, C.D., (1997) Structure (London), 5, 763. | ||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 110 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: FUJI / Detector: IMAGE PLATE / Date: Nov 15, 1996 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength![]() |
Reflection | Resolution: 2.1→20 Å / Num. obs: 17675 / % possible obs: 79.6 % / Observed criterion σ(I): 2 / Redundancy: 8 % / Rmerge(I) obs: 0.064 |
Reflection | *PLUS Num. measured all: 167167 |
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Processing
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Refinement | Resolution: 2.6→10 Å / Data cutoff high absF: 100000 / Data cutoff low absF: 0.1 / σ(F): 2
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Displacement parameters | Biso mean: 42.9 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.6→10 Å
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Refine LS restraints |
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Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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