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Open data
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Basic information
Entry | Database: PDB / ID: 2fit | ||||||
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Title | FHIT (FRAGILE HISTIDINE TRIAD PROTEIN) | ||||||
![]() | FRAGILE HISTIDINE PROTEIN | ||||||
![]() | CHROMOSOMAL TRANSLOCATION / FHIT / FRAGILE HISTIDINE TRIAD PROTEIN / PUTATIVE HUMAN TUMOR SUPPRESSOR / ADVANCED PHOTON SOURCE / APS / HIT PROTEIN FAMILY / PKCI | ||||||
Function / homology | ![]() adenylylsulfate-ammonia adenylyltransferase / adenylylsulfatase / diadenosine triphosphate catabolic process / adenylylsulfate-ammonia adenylyltransferase activity / bis(5'-adenosyl)-triphosphatase / bis(5'-adenosyl)-triphosphatase activity / purine nucleotide metabolic process / adenylylsulfatase activity / Hydrolases; Acting on phosphorus-nitrogen bonds / adenosine 5'-monophosphoramidase activity ...adenylylsulfate-ammonia adenylyltransferase / adenylylsulfatase / diadenosine triphosphate catabolic process / adenylylsulfate-ammonia adenylyltransferase activity / bis(5'-adenosyl)-triphosphatase / bis(5'-adenosyl)-triphosphatase activity / purine nucleotide metabolic process / adenylylsulfatase activity / Hydrolases; Acting on phosphorus-nitrogen bonds / adenosine 5'-monophosphoramidase activity / intrinsic apoptotic signaling pathway by p53 class mediator / negative regulation of proteasomal ubiquitin-dependent protein catabolic process / fibrillar center / nucleotide binding / ubiquitin protein ligase binding / mitochondrion / identical protein binding / nucleus / plasma membrane / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Lima, C.D. / D'Amico, K.L. / Naday, I. / Rosenbaum, G. / Westbrook, E.M. / Hendrickson, W.A. | ||||||
![]() | ![]() 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 | ![]() | 37.5 KB | Display | ![]() |
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PDB format | ![]() | 28.6 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 395.6 KB | Display | ![]() |
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Full document | ![]() | 397 KB | Display | |
Data in XML | ![]() | 4.6 KB | Display | |
Data in CIF | ![]() | 7.1 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-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: 16979.992 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Details: SELENOMETHIONYL FHIT WITH BOUND SULFATE IN ACTIVE SITE Source: (gene. exp.) ![]() Description: EXPRESSED AS FUSION PROTEIN WITH GLUTATHIONE-S-TRANSFERASE Gene: FHIT / Plasmid: PGEX-2T / Gene (production host): FHIT / Production host: ![]() ![]() | ||
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#2: Sugar | ChemComp-FRU / | ||
#3: Chemical | #4: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.91 Å3/Da / Density % sol: 57.8 % Description: DATA WERE COLLECTED USING 0.2 DEGREE OSCILLATIONS BY CONTINUOUSLY ADDING PARTIALS. | ||||||||||||||||||||
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Crystal grow | pH: 6.5 / Details: 1.25-1.35M AMSO4, 100MM SODIUM CACODYLATE PH6.5 | ||||||||||||||||||||
Crystal grow | *PLUS Method: unknown | ||||||||||||||||||||
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: CUSTOM-MADE / Detector: CCD / Date: May 23, 1996 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9639 Å / Relative weight: 1 |
Reflection | Highest resolution: 1.7 Å / Num. obs: 30590 / % possible obs: 68.2 % / Observed criterion σ(I): 2 / Redundancy: 3 % / Rmerge(I) obs: 0.039 |
Reflection | *PLUS Num. measured all: 89229 |
Reflection shell | *PLUS % possible obs: 31 % / Rmerge(I) obs: 0.188 |
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Processing
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Refinement | Method to determine structure: ![]()
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Displacement parameters | Biso mean: 27.5 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.9→8 Å
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Refine LS restraints |
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Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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