+Open data
-Basic information
Entry | Database: PDB / ID: 1g0b | ||||||
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Title | CARBONMONOXY LIGANDED EQUINE HEMOGLOBIN PH 8.5 | ||||||
Components |
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Keywords | OXYGEN STORAGE/TRANSPORT / equine / hemoglobin / liganded / carbonmonoxy / protoporphyrin IX / OXYGEN STORAGE-TRANSPORT COMPLEX | ||||||
Function / homology | Function and homology information cellular oxidant detoxification / hemoglobin alpha binding / haptoglobin-hemoglobin complex / organic acid binding / hemoglobin complex / hydrogen peroxide catabolic process / oxygen carrier activity / oxygen binding / iron ion binding / heme binding / metal ion binding Similarity search - Function | ||||||
Biological species | Equus caballus (horse) | ||||||
Method | X-RAY DIFFRACTION / Resolution: 1.9 Å | ||||||
Authors | Mueser, T.C. / Rogers, P.H. / Arnone, A. | ||||||
Citation | Journal: Biochemistry / Year: 2000 Title: Interface sliding as illustrated by the multiple quaternary structures of liganded hemoglobin. Authors: Mueser, T.C. / Rogers, P.H. / Arnone, A. #1: Journal: J.Mol.Biol. / Year: 1977 Title: The structure of horse methaemoglobin at 2-0 A resolution. Authors: Ladner, R.C. / Heidner, E.J. / Perutz, M.F. | ||||||
History |
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Remark 999 | SEQUENCE The sequence is the same as in pdb entry 2MHB. This 1g0b structure is a re-refined ...SEQUENCE The sequence is the same as in pdb entry 2MHB. This 1g0b structure is a re-refined structure of R.C.LADNER,E.G.HEIDNER,M.F.PERUTZ from 1977. |
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1g0b.cif.gz | 70.7 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1g0b.ent.gz | 53.5 KB | Display | PDB format |
PDBx/mmJSON format | 1g0b.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/g0/1g0b ftp://data.pdbj.org/pub/pdb/validation_reports/g0/1g0b | HTTPS FTP |
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-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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Details | The biological assembly is a tetramer constructed from the heterodimer of chain A (alpha) and chain B (beta) and a symmetry related heterodimer of chain A (alpha) and chain B (beta) |
-Components
#1: Protein | Mass: 15138.280 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Equus caballus (horse) / Tissue: BLOOD / References: UniProt: P01958 | ||||
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#2: Protein | Mass: 16032.274 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Equus caballus (horse) / Tissue: BLOOD / References: UniProt: P02062 | ||||
#3: Chemical | #4: Chemical | #5: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.82 Å3/Da / Density % sol: 56.33 % / Description: AUTHOR USED THE SF DATA FROM ENTRY 2MHB. | |||||||||||||||
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Crystal grow | *PLUS | |||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Radiation | Scattering type: x-ray |
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Radiation wavelength | Relative weight: 1 |
Reflection | *PLUS Num. measured all: 316145 |
Reflection shell | *PLUS % possible obs: 87.8 % |
-Processing
Software |
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Refinement | Resolution: 1.9→8 Å / σ(F): 2 / σ(I): 0 / Stereochemistry target values: Engh & Huber
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Refinement step | Cycle: LAST / Resolution: 1.9→8 Å
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Refine LS restraints |
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Software | *PLUS Name: PROLSQ / Classification: refinement | ||||||||||||||||
Refinement | *PLUS | ||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||
Displacement parameters | *PLUS Biso mean: 24.8 Å2 |