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Yorodumi- PDB-1hco: THE STRUCTURE OF HUMAN CARBONMONOXY HAEMOGLOBIN AT 2.7 ANGSTROMS ... -
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Open data
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Basic information
| Entry | Database: PDB / ID: 1hco | |||||||||
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| Title | THE STRUCTURE OF HUMAN CARBONMONOXY HAEMOGLOBIN AT 2.7 ANGSTROMS RESOLUTION | |||||||||
Components |
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Keywords | OXYGEN TRANSPORT | |||||||||
| Function / homology | Function and homology informationnitric oxide transport / hemoglobin alpha binding / cellular oxidant detoxification / hemoglobin binding / haptoglobin-hemoglobin complex / renal absorption / hemoglobin complex / oxygen transport / Scavenging of heme from plasma / endocytic vesicle lumen ...nitric oxide transport / hemoglobin alpha binding / cellular oxidant detoxification / hemoglobin binding / haptoglobin-hemoglobin complex / 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 / carbon dioxide transport / response to hydrogen peroxide / Heme signaling / Erythrocytes take up oxygen and release carbon dioxide / Erythrocytes take up carbon dioxide and release oxygen / Late endosomal microautophagy / Cytoprotection by HMOX1 / oxygen binding / regulation of blood pressure / platelet aggregation / Chaperone Mediated Autophagy / positive regulation of nitric oxide biosynthetic process / tertiary granule lumen / Factors involved in megakaryocyte development and platelet production / blood microparticle / ficolin-1-rich granule lumen / iron ion binding / inflammatory response / heme binding / Neutrophil degranulation / extracellular space / extracellular exosome / extracellular region / metal ion binding / membrane / cytosol Similarity search - Function | |||||||||
| Biological species | Homo sapiens (human) | |||||||||
| Method | X-RAY DIFFRACTION / Resolution: 2.7 Å | |||||||||
Authors | Baldwin, J.M. | |||||||||
Citation | Journal: J.Mol.Biol. / Year: 1980Title: The structure of human carbonmonoxy haemoglobin at 2.7 A resolution. Authors: Baldwin, J.M. #1: Journal: J.Mol.Biol. / Year: 1979Title: Haemoglobin. The Structural Changes Related to Ligand Binding and its Allosteric Mechanism Authors: Baldwin, J. / Chothia, C. | |||||||||
| History |
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Structure visualization
| Structure viewer | Molecule: Molmil Jmol/JSmol |
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Downloads & links
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Download
| PDBx/mmCIF format | 1hco.cif.gz | 64.4 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb1hco.ent.gz | 43.7 KB | Display | PDB format |
| PDBx/mmJSON format | 1hco.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/hc/1hco ftp://data.pdbj.org/pub/pdb/validation_reports/hc/1hco | 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: 15150.353 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / References: UniProt: P69905 | ||
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| #2: Protein | Mass: 15890.198 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / References: UniProt: P68871 | ||
| #3: Chemical | | #4: Chemical | |
-Experimental details
-Experiment
| Experiment | Method: X-RAY DIFFRACTION |
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Sample preparation
| Crystal | Density Matthews: 2.24 Å3/Da / Density % sol: 45.09 % |
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| Crystal grow | *PLUS pH: 6.6 / Method: unknown |
| Components of the solutions | *PLUS Conc.: 2.2 M / Common name: phosphate |
-Data collection
| Radiation | Scattering type: x-ray |
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| Radiation wavelength | Relative weight: 1 |
| Reflection | *PLUS Highest resolution: 2.7 Å / Num. obs: 8020 / Num. measured all: 27806 / Rmerge(I) obs: 0.049 |
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Processing
| Refinement | Highest resolution: 2.7 Å | ||||||||||||
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| Refinement step | Cycle: LAST / Highest resolution: 2.7 Å
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Homo sapiens (human)
X-RAY DIFFRACTION
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