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- PDB-2pgh: STRUCTURE DETERMINATION OF AQUOMET PORCINE HEMOGLOBIN AT 2.8 ANGS... -
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Open data
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Basic information
Entry | Database: PDB / ID: 2pgh | |||||||||
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Title | STRUCTURE DETERMINATION OF AQUOMET PORCINE HEMOGLOBIN AT 2.8 ANGSTROM RESOLUTION | |||||||||
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![]() | OXYGEN TRANSPORT | |||||||||
Function / homology | ![]() cellular oxidant detoxification / hemoglobin alpha binding / haptoglobin-hemoglobin complex / organic acid binding / hemoglobin complex / hydrogen peroxide catabolic process / oxygen carrier activity / oxygen binding / iron ion binding / heme binding / metal ion binding Similarity search - Function | |||||||||
Biological species | ![]() ![]() | |||||||||
Method | ![]() | |||||||||
![]() | Katz, D.S. / White, S.P. / Huang, W. / Kumar, R. / Christianson, D.W. | |||||||||
![]() | ![]() Title: Structure determination of aquomet porcine hemoglobin at 2.8 A resolution. Authors: Katz, D.S. / White, S.P. / Huang, W. / Kumar, R. / Christianson, D.W. #1: ![]() Title: Production of Hemoglobin in Transgenic Swine: An Approach to a Blood Substitute Authors: O'Donnell, J.K. / Martin, M.J. / Logan, J.S. / Kumar, R. #2: ![]() Title: The Purification and Comparative Analysis of Hemoglobin from Animal Bloods Authors: Lee, C.J. / Kan, P. / Chen, W.K. #3: ![]() Title: Production of Functional Human Hemoglobin in Transgenic Swine Authors: Swanson, M.E. / Martin, M.J. / O'Donnell, J.K. / Hoover, K. / Sago, W. / Huntress, V. / Parsons, C.T. / Pinkert, C.A. / Pilder, S. / Logan, J.S. | |||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 126.2 KB | Display | ![]() |
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PDB format | ![]() | 99.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 15064.144 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() #2: Protein | Mass: 16059.345 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() #3: Chemical | ChemComp-HEM / #4: Water | ChemComp-HOH / | Compound details | THE DEPOSITORS CONCLUDE THAT THEIR CRYSTALS ARE OF AQUOMET FORM BECAUSE: A) PRECAUTIONS SIMILAR TO ...THE DEPOSITORS | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.36 Å3/Da / Density % sol: 47.79 % | ||||||||||||||||||||||||||||
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Crystal grow | *PLUS pH: 7 / Method: vapor diffusion, hanging drop | ||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Reflection | *PLUS Highest resolution: 2.8 Å / Num. obs: 13290 / Num. measured all: 44042 / Rmerge(I) obs: 0.087 |
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Processing
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Refinement | Resolution: 2.8→6.5 Å / σ(F): 2 /
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Refinement step | Cycle: LAST / Resolution: 2.8→6.5 Å
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Refine LS restraints |
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Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Rfactor obs: 0.154 / Rfactor Rfree: 0.295 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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