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Open data
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Basic information
Entry | Database: PDB / ID: 1c7d | ||||||
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Title | DEOXY RHB1.2 (RECOMBINANT HEMOGLOBIN) | ||||||
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![]() | OXYGEN STORAGE/TRANSPORT / HEME / OXYGEN DELIVERY VEHICLE / BLOOD SUBSTITUTE / OXYGEN STORAGE-TRANSPORT COMPLEX | ||||||
Function / homology | ![]() nitric oxide transport / cellular oxidant detoxification / hemoglobin binding / hemoglobin alpha binding / haptoglobin-hemoglobin complex / organic acid binding / renal absorption / hemoglobin complex / oxygen transport / Scavenging of heme from plasma ...nitric oxide transport / cellular oxidant detoxification / hemoglobin binding / hemoglobin alpha binding / haptoglobin-hemoglobin complex / organic acid binding / renal absorption / hemoglobin complex / oxygen transport / Scavenging of heme from plasma / endocytic vesicle lumen / blood vessel diameter maintenance / hydrogen peroxide catabolic process / oxygen carrier activity / Late endosomal microautophagy / Heme signaling / carbon dioxide transport / Erythrocytes take up oxygen and release carbon dioxide / response to hydrogen peroxide / Erythrocytes take up carbon dioxide and release oxygen / Cytoprotection by HMOX1 / platelet aggregation / oxygen binding / regulation of blood pressure / Chaperone Mediated Autophagy / positive regulation of nitric oxide biosynthetic process / tertiary granule lumen / Factors involved in megakaryocyte development and platelet production / ficolin-1-rich granule lumen / blood microparticle / iron ion binding / heme binding / Neutrophil degranulation / extracellular space / extracellular exosome / extracellular region / membrane / metal ion binding / cytosol Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Brucker, E.A. | ||||||
![]() | ![]() Title: Genetically crosslinked hemoglobin: a structural study. Authors: Brucker, E.A. #1: ![]() Title: Structures of a Hemoglobin-Based Blood Substitute: Insights Into the Function of Allosteric Proteins Authors: Kroeger, K.S. / Kundrot, C.E. #2: ![]() Title: A Human Recombinant Haemoglobin Designed for Use as a Blood Substitute Authors: Looker, D. / Abbot-Brown, D. / Cozart, P. / Durfee, S. / Hoffman, S. / Mathews, A.J. / Miller-Roehrich, J. / Shoemaker, S. / Trimble, S. / Fermi, G. / Komiyama, N.H. / Nagai, K. / Stetler, G.L. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 131.5 KB | Display | ![]() |
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PDB format | ![]() | 101.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 1c7bC ![]() 1c7cC ![]() 1abyS C: citing same article ( S: Starting model for refinement |
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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: 30428.895 Da / Num. of mol.: 1 / Mutation: V1M,142G,143G Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() | ||||
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#2: Protein | Mass: 15937.343 Da / Num. of mol.: 2 / Mutation: V1M,N108K Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() #3: Chemical | ChemComp-HEM / #4: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 1.84 Å3/Da / Density % sol: 33.3 % |
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Crystal grow | pH: 6.5 / Details: PERUTZ, J.CRYST.GROWTH 2(1968)54-56, pH 6.5 |
Crystal grow | *PLUS Method: batch method / pH: 7 |
Components of the solutions | *PLUS Conc.: 10 mM / Common name: ammonium phosphate |
-Data collection
Diffraction | Mean temperature: 295 K |
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Diffraction source | Source: ![]() |
Detector | Type: RIGAKU RAXIS IIC / Detector: IMAGE PLATE / Date: Dec 15, 1998 / Details: COLLIMATOR |
Radiation | Monochromator: GRAPHITE / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 1.8→30 Å / Num. obs: 45959 / % possible obs: 90.2 % / Redundancy: 2.91 % / Rmerge(I) obs: 0.065 / Net I/σ(I): 11.3 |
Reflection shell | Resolution: 1.8→1.9 Å / Redundancy: 2.86 % / Rmerge(I) obs: 0.241 / Mean I/σ(I) obs: 4.42 / % possible all: 87.4 |
Reflection | *PLUS Redundancy: 2.9 % / Num. measured all: 133741 |
Reflection shell | *PLUS % possible obs: 87.4 % / Redundancy: 2.9 % / Mean I/σ(I) obs: 4.4 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 1ABY Resolution: 1.8→8 Å / Num. parameters: 19271 / Num. restraintsaints: 28895 / Cross valid method: FREE R / σ(F): 0 / Stereochemistry target values: ENGH AND HUBER
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Solvent computation | Solvent model: MOEWS & KRETSINGER, J.MOL.BIOL. 91(1973)201-228 | |||||||||||||||||||||||||||||||||
Refine analyze | Num. disordered residues: 0 / Occupancy sum hydrogen: 0 / Occupancy sum non hydrogen: 4802 | |||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.8→8 Å
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Refine LS restraints |
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Software | *PLUS Name: SHELXL / Version: 97 / Classification: refinement | |||||||||||||||||||||||||||||||||
Refinement | *PLUS Rfactor Rwork: 0.188 / Lowest resolution: 8 Å / Num. reflection obs: 45496 / % reflection Rfree: 4.7 % / Rfactor obs: 0.189 / Rfactor Rfree: 0.24 | |||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | |||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | |||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS Type: s_chiral_restr / Dev ideal: 0.034 |