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- PDB-5uys: Human steroidogenic cytochrome P450 17A1 with 3alphaOH-5alpha-abi... -
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Open data
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Basic information
Entry | Database: PDB / ID: 5uys | ||||||
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Title | Human steroidogenic cytochrome P450 17A1 with 3alphaOH-5alpha-abiraterone analog | ||||||
![]() | Steroid 17-alpha-hydroxylase/17,20 lyase | ||||||
![]() | OXIDOREDUCTASE / Steroidogenic | ||||||
Function / homology | ![]() Defective CYP17A1 causes AH5 / steroid 17alpha-monooxygenase / 17alpha-hydroxyprogesterone deacetylase / steroid 17-alpha-monooxygenase activity / : / glucocorticoid biosynthetic process / Androgen biosynthesis / hormone biosynthetic process / Glucocorticoid biosynthesis / androgen biosynthetic process ...Defective CYP17A1 causes AH5 / steroid 17alpha-monooxygenase / 17alpha-hydroxyprogesterone deacetylase / steroid 17-alpha-monooxygenase activity / : / glucocorticoid biosynthetic process / Androgen biosynthesis / hormone biosynthetic process / Glucocorticoid biosynthesis / androgen biosynthetic process / sex differentiation / progesterone metabolic process / steroid biosynthetic process / steroid metabolic process / oxygen binding / iron ion binding / axon / neuronal cell body / endoplasmic reticulum membrane / heme binding / endoplasmic reticulum Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Scott, E.E. / Petrunak, E.M. | ||||||
Funding support | ![]()
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![]() | ![]() Title: Human cytochrome P450 17A1 structures with metabolites of prostate cancer drug abiraterone reveal substrate-binding plasticity and a second binding site. Authors: Petrunak, E.M. / Bart, A.G. / Peng, H.M. / Auchus, R.J. / Scott, E.E. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 719.9 KB | Display | ![]() |
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PDB format | ![]() | 606.5 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 6wr0C ![]() 6wr1C ![]() 6ww0C ![]() 3swzS S: Starting model for refinement C: citing same article ( |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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4 | ![]()
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Unit cell |
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Details | Monomer as determined by gel filtration |
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Components
#1: Protein | Mass: 55740.141 Da / Num. of mol.: 4 / Fragment: residues 24-508 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() References: UniProt: P05093, steroid 17alpha-monooxygenase, 17alpha-hydroxyprogesterone deacetylase #2: Chemical | ChemComp-HEM / #3: Chemical | ChemComp-8QD / ( #4: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.6 Å3/Da / Density % sol: 52.76 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop Details: 175 mM Tris HCl, pH 8.5, 30% PEG-3350, 300 mM LiSO4, 3% glycerol |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MARMOSAIC 325 mm CCD / Detector: CCD / Date: Jul 19, 2013 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.98 Å / Relative weight: 1 |
Reflection | Resolution: 2.39→39.29 Å / Num. obs: 92392 / % possible obs: 99.8 % / Redundancy: 7.4 % / Rpim(I) all: 0.067 / Net I/σ(I): 11.5 |
Reflection shell | Resolution: 2.39→2.52 Å / Redundancy: 7.4 % / Mean I/σ(I) obs: 1.5 / Num. unique obs: 13193 / % possible all: 98.6 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 3SWZ Resolution: 2.392→39.286 Å / SU ML: 0.34 / Cross valid method: FREE R-VALUE / σ(F): 1.34 / Phase error: 26.76
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å | ||||||||||||||||||||||||
Displacement parameters | Biso max: 167.7 Å2 / Biso mean: 42.63 Å2 / Biso min: 14.16 Å2 | ||||||||||||||||||||||||
Refinement step | Cycle: final / Resolution: 2.392→39.286 Å
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Refine LS restraints | Type: f_bond_d / Dev ideal: 0.007 / Number: 15663 | ||||||||||||||||||||||||
LS refinement shell | Resolution: 2.3921→2.4193 Å / Rfactor Rfree error: 0
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