+Open data
-Basic information
Entry | Database: PDB / ID: 1z8u | ||||||
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Title | Crystal structure of oxidized alpha hemoglobin bound to AHSP | ||||||
Components |
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Keywords | ELECTRON TRANSPORT / alpha haemoglobin / AHSP / oxidation / interaction | ||||||
Function / homology | Function and homology information hemoglobin metabolic process / cellular oxidant detoxification / nitric oxide transport / haptoglobin-hemoglobin complex / hemoglobin binding / organic acid binding / hemoglobin complex / hemopoiesis / oxygen transport / Scavenging of heme from plasma ...hemoglobin metabolic process / cellular oxidant detoxification / nitric oxide transport / haptoglobin-hemoglobin complex / hemoglobin binding / organic acid binding / hemoglobin complex / hemopoiesis / oxygen transport / Scavenging of heme from plasma / endocytic vesicle lumen / erythrocyte differentiation / hydrogen peroxide catabolic process / oxygen carrier activity / 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 / oxygen binding / unfolded protein binding / protein folding / blood microparticle / protein stabilization / iron ion binding / heme binding / extracellular space / extracellular exosome / extracellular region / membrane / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MAD / Resolution: 2.4 Å | ||||||
Authors | Feng, L. / Zhou, S. / Gu, L. / Gell, D.A. / Mackay, J.P. / Weiss, M.J. / Gow, A.J. / Shi, Y. | ||||||
Citation | Journal: Nature / Year: 2005 Title: Structure of oxidized alpha-haemoglobin bound to AHSP reveals a protective mechanism for haem. Authors: Feng, L. / Zhou, S. / Gu, L. / Gell, D.A. / Mackay, J.P. / Weiss, M.J. / Gow, A.J. / Shi, Y. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1z8u.cif.gz | 112 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1z8u.ent.gz | 86.2 KB | Display | PDB format |
PDBx/mmJSON format | 1z8u.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/z8/1z8u ftp://data.pdbj.org/pub/pdb/validation_reports/z8/1z8u | HTTPS FTP |
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-Related structure data
Related structure data | |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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2 |
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3 |
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Unit cell |
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Components on special symmetry positions |
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-Components
#1: Protein | Mass: 11826.327 Da / Num. of mol.: 2 / Mutation: P30A Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: AHSP, EDRF, ERAF / Production host: Escherichia coli (E. coli) / References: UniProt: Q9NZD4 #2: Protein | Mass: 15281.550 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: HBA1 / Production host: Escherichia coli (E. coli) / References: UniProt: P69905 #3: Chemical | #4: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.4 Å3/Da / Density % sol: 50 % |
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Crystal grow | Temperature: 277 K / Method: vapor diffusion, hanging drop / pH: 6.5 Details: MES, PEG-2000 monomethyl ether, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K |
-Data collection
Diffraction | Mean temperature: 100 K | ||||||||||||
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Diffraction source | Source: SYNCHROTRON / Site: NSLS / Beamline: X25 / Wavelength: 1.7319, 1.7338, 1.7 | ||||||||||||
Detector | Type: ADSC QUANTUM 4 / Detector: CCD / Date: Aug 20, 2004 | ||||||||||||
Radiation | Monochromator: X25 / Protocol: MAD / Monochromatic (M) / Laue (L): M / Scattering type: x-ray | ||||||||||||
Radiation wavelength |
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Reflection | Resolution: 2.4→99 Å / Num. all: 23106 / Num. obs: 22990 / % possible obs: 99.5 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Rsym value: 0.058 / Net I/σ(I): 20.9 | ||||||||||||
Reflection shell | Resolution: 2.4→2.49 Å / Rmerge(I) obs: 0.27 / Mean I/σ(I) obs: 4.5 / Rsym value: 0.27 / % possible all: 99.4 |
-Processing
Software |
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Refinement | Method to determine structure: MAD / Resolution: 2.4→20 Å / σ(F): 0 / σ(I): 0 / Stereochemistry target values: Engh & Huber
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Refinement step | Cycle: LAST / Resolution: 2.4→20 Å
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Refine LS restraints |
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