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Yorodumi- PDB-1coh: STRUCTURE OF HAEMOGLOBIN IN THE DEOXY QUATERNARY STATE WITH LIGAN... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1coh | |||||||||
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Title | STRUCTURE OF HAEMOGLOBIN IN THE DEOXY QUATERNARY STATE WITH LIGAND BOUND AT THE ALPHA HAEMS | |||||||||
Components |
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Keywords | OXYGEN TRANSPORT | |||||||||
Function / homology | Function and homology information nitric oxide transport / hemoglobin binding / hemoglobin alpha binding / haptoglobin binding / haptoglobin-hemoglobin complex / organic acid binding / renal absorption / hemoglobin complex / oxygen transport / Scavenging of heme from plasma ...nitric oxide transport / hemoglobin binding / hemoglobin alpha binding / haptoglobin 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 / 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 / iron ion binding / heme binding / Neutrophil degranulation / extracellular space / extracellular exosome / extracellular region / membrane / metal ion binding / cytosol Similarity search - Function | |||||||||
Biological species | Homo sapiens (human) | |||||||||
Method | X-RAY DIFFRACTION / Resolution: 2.9 Å | |||||||||
Authors | Luisi, B. | |||||||||
Citation | Journal: J.Mol.Biol. / Year: 1989 Title: Structure of haemoglobin in the deoxy quaternary state with ligand bound at the alpha haems. Authors: Luisi, B. / Shibayama, N. #1: Journal: Acc.Chem.Res. / Year: 1987 Title: Stereochemistry of Cooperative Mechanisms in Hemoglobin Authors: Perutz, M.F. / Fermi, G. / Luisi, B. / Shaanan, B. / Liddington, R.C. | |||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1coh.cif.gz | 126.8 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1coh.ent.gz | 98.6 KB | Display | PDB format |
PDBx/mmJSON format | 1coh.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1coh_validation.pdf.gz | 708 KB | Display | wwPDB validaton report |
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Full document | 1coh_full_validation.pdf.gz | 716.1 KB | Display | |
Data in XML | 1coh_validation.xml.gz | 13.7 KB | Display | |
Data in CIF | 1coh_validation.cif.gz | 21.5 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/co/1coh ftp://data.pdbj.org/pub/pdb/validation_reports/co/1coh | HTTPS FTP |
-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
-Protein , 2 types, 4 molecules ACBD
#1: Protein | Mass: 15150.353 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / References: UniProt: P69905 #2: Protein | Mass: 15890.198 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / References: UniProt: P68871 |
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-Non-polymers , 4 types, 203 molecules
#3: Chemical | #4: Chemical | #5: Chemical | #6: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 2.23 Å3/Da / Density % sol: 44.9 % |
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Crystal grow | *PLUS Method: other |
Components of the solutions | *PLUS Conc.: 2.45-2.55 M / Common name: ammonium sulfate |
-Data collection
Radiation | Scattering type: x-ray |
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Radiation wavelength | Relative weight: 1 |
Reflection | *PLUS Highest resolution: 2.9 Å / Num. obs: 11733 / Num. measured all: 55367 / Rmerge(I) obs: 0.108 |
-Processing
Software | Name: EREF / Classification: refinement | ||||||||||||
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Refinement | Highest resolution: 2.9 Å | ||||||||||||
Refinement step | Cycle: LAST / Highest resolution: 2.9 Å
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