+Open data
-Basic information
Entry | Database: PDB / ID: 1oxa | ||||||
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Title | CYTOCHROME P450 (DONOR:O2 OXIDOREDUCTASE) | ||||||
Components | CYTOCHROME P450 ERYF | ||||||
Keywords | OXIDOREDUCTASE (OXYGENASE) | ||||||
Function / homology | Function and homology information 6-deoxyerythronolide B hydroxylase / erythromycin biosynthetic process / cholest-4-en-3-one 26-monooxygenase activity / steroid hydroxylase activity / cholesterol catabolic process / monooxygenase activity / iron ion binding / heme binding / cytoplasm Similarity search - Function | ||||||
Biological species | Saccharopolyspora erythraea (bacteria) | ||||||
Method | X-RAY DIFFRACTION / Resolution: 2.1 Å | ||||||
Authors | Cupp-Vickery, J.R. / Poulos, T.L. | ||||||
Citation | Journal: Nat.Struct.Biol. / Year: 1995 Title: Structure of cytochrome P450eryF involved in erythromycin biosynthesis. Authors: Cupp-Vickery, J.R. / Poulos, T.L. #1: Journal: Proteins / Year: 1994 Title: Preliminary Crystallographic Analysis of an Enzyme Involved in Erythromycin Biosynthesis: Cytochrome P450Eryf Authors: Cupp-Vickery, J.R. / Li, H. / Poulos, T.L. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1oxa.cif.gz | 98.2 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1oxa.ent.gz | 72.9 KB | Display | PDB format |
PDBx/mmJSON format | 1oxa.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1oxa_validation.pdf.gz | 556.1 KB | Display | wwPDB validaton report |
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Full document | 1oxa_full_validation.pdf.gz | 560.8 KB | Display | |
Data in XML | 1oxa_validation.xml.gz | 9.9 KB | Display | |
Data in CIF | 1oxa_validation.cif.gz | 15.7 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ox/1oxa ftp://data.pdbj.org/pub/pdb/validation_reports/ox/1oxa | 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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Atom site foot note | 1: CIS PROLINE - PRO 96 |
-Components
#1: Protein | Mass: 44515.152 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Saccharopolyspora erythraea (bacteria) / References: UniProt: Q00441 |
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#2: Chemical | ChemComp-HEM / |
#3: Chemical | ChemComp-DEB / |
#4: 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: 2.41 Å3/Da / Density % sol: 48.95 % Description: TWO DERIVATIVE DATA SETS WERE ACQUIRED WITH A SIEMENS X-1000 AREA DETECTOR AND A ROTATING ANODE EQUIPPED WITH FOCUSING, MIRROR OPTICS. A NATIVE DATA SET WAS COLLECTED WITH TWO MARK III ...Description: TWO DERIVATIVE DATA SETS WERE ACQUIRED WITH A SIEMENS X-1000 AREA DETECTOR AND A ROTATING ANODE EQUIPPED WITH FOCUSING, MIRROR OPTICS. A NATIVE DATA SET WAS COLLECTED WITH TWO MARK III AREA DETECTORS AND A RIGAKU ROTATING ANODE AT THE UNIVERSITY OF CALIFORNIA, SAN DIEGO, U.S.A. | ||||||||||||||||||||
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Crystal grow | *PLUS pH: 8.5 / Method: vapor diffusion, hanging drop | ||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction source | Wavelength: 1.5418 Å |
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Detector | Type: SIEMENS-NICOLET X100 / Detector: AREA DETECTOR |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Highest resolution: 2.1 Å / Num. obs: 23771 / % possible obs: 91 % / Observed criterion σ(I): 0 / Rmerge(I) obs: 0.0538 |
Reflection | *PLUS Num. measured all: 127949 / Rmerge(I) obs: 0.0538 |
-Processing
Software |
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Refinement | Resolution: 2.1→10 Å / Rfactor Rwork: 0.196 / Rfactor obs: 0.196 / σ(F): 0 Details: RESIDUES 160 - 166 WERE NOT VISIBLE IN THE ELECTRON DENSITY. RESIDUE NUMBER 1 IS NOT VISIBLE. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.1→10 Å
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Refine LS restraints |
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Software | *PLUS Name: X-PLOR / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS |