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Open data
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Basic information
Entry | Database: PDB / ID: 1ch4 | ||||||
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Title | MODULE-SUBSTITUTED CHIMERA HEMOGLOBIN BETA-ALPHA (F133V) | ||||||
![]() | MODULE-SUBSTITUTED CHIMERA HEMOGLOBIN BETA-ALPHA | ||||||
![]() | OXYGEN TRANSPORT / CHIMERA PROTEIN / RESPIRATORY PROTEIN / HEME | ||||||
Function / homology | ![]() nitric oxide transport / hemoglobin binding / hemoglobin alpha binding / haptoglobin binding / haptoglobin-hemoglobin complex / renal absorption / organic acid binding / hemoglobin complex / oxygen transport / Scavenging of heme from plasma ...nitric oxide transport / hemoglobin binding / hemoglobin alpha binding / haptoglobin binding / haptoglobin-hemoglobin complex / renal absorption / organic acid binding / 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 / response to hydrogen peroxide / Erythrocytes take up oxygen and release carbon dioxide / Erythrocytes take up carbon dioxide and release oxygen / Cytoprotection by HMOX1 / oxygen binding / regulation of blood pressure / platelet aggregation / Chaperone Mediated Autophagy / peroxidase activity / 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 / heme binding / Neutrophil degranulation / extracellular space / extracellular exosome / extracellular region / metal ion binding / cytosol Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Shirai, T. / Fujikake, M. / Yamane, T. / Inaba, K. / Ishimori, K. / Morishima, I. | ||||||
![]() | ![]() Title: Crystal structure of a protein with an artificial exon-shuffling, module M4-substituted chimera hemoglobin beta alpha, at 2.5 A resolution. Authors: Shirai, T. / Fujikake, M. / Yamane, T. / Inaba, K. / Ishimori, K. / Morishima, I. #1: ![]() Title: Design, Construction, Crystallization, and Preliminary X-Ray Studies of a Fine-Tuning Mutant (F133V) of Module-Substituted Chimera Hemoglobin Authors: Shirai, T. / Fujikake, M. / Yamane, T. / Inaba, K. / Ishimori, K. / Morishima, I. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 127.2 KB | Display | ![]() |
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PDB format | ![]() | 100.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 689.2 KB | Display | ![]() |
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Full document | ![]() | 706.4 KB | Display | |
Data in XML | ![]() | 15.4 KB | Display | |
Data in CIF | ![]() | 20.2 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar 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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Noncrystallographic symmetry (NCS) | NCS oper: (Code: given Matrix: (-0.908143, -0.144029, -0.393105), Vector: Details | THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT IS THE CHIMERA-TETRAMER. | |
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Components
#1: Protein | Mass: 15812.229 Da / Num. of mol.: 4 / Mutation: F133V Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() #2: Chemical | ChemComp-HEM / #3: Chemical | ChemComp-CMO / #4: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.23 Å3/Da / Density % sol: 44.74 % | |||||||||||||||||||||||||
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Crystal grow | pH: 6.5 / Details: pH 6.5 | |||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 18 ℃ / pH: 7 / Method: vapor diffusion, hanging dropDetails: Shirai, T., (1998) Proteins: Struct.,Funct., Genet., 32, 263. | |||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 291 K |
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Diffraction source | Source: ![]() |
Detector | Type: MACSCIENCE / Detector: IMAGE PLATE / Date: Oct 1, 1996 / Details: MIRRORS |
Radiation | Monochromator: NI FILTER / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.5→20 Å / Num. obs: 17766 / % possible obs: 91.2 % / Observed criterion σ(I): 1 / Redundancy: 4.9 % / Rmerge(I) obs: 0.088 / Net I/σ(I): 5.6 |
Reflection shell | Resolution: 2.5→2.59 Å / % possible all: 82.5 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: CN-HEMOGLOBIN H Resolution: 2.5→8 Å / Cross valid method: THROUGHOUT / σ(F): 3 Details: THIS PROTEIN WAS CONSTRUCTED BY REPLACING MODULE M4, 97(FG4)-146(HC3), OF BETA-SUBUNIT OF HUMAN HEMOGLOBIN WITH THE CORRESPONDING REGION, 92(FG4)-141(HC3), OF THE ALPHA-SUBUNIT. A POINT ...Details: THIS PROTEIN WAS CONSTRUCTED BY REPLACING MODULE M4, 97(FG4)-146(HC3), OF BETA-SUBUNIT OF HUMAN HEMOGLOBIN WITH THE CORRESPONDING REGION, 92(FG4)-141(HC3), OF THE ALPHA-SUBUNIT. A POINT MUTATION F133V(H11) WAS INTRODUCED TO INCREASE THE STABILITY.
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Displacement parameters | Biso mean: 27.9 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine analyze | Luzzati coordinate error obs: 0.25 Å / Luzzati d res low obs: 7 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.5→8 Å
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Refine LS restraints |
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Refine LS restraints NCS | NCS model details: STRICT | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Xplor file |
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Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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