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Open data
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Basic information
Entry | Database: PDB / ID: 7chx | |||||||||||||||
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Title | acylphosphatase from Staphylococcus aureus | |||||||||||||||
![]() | Acylphosphatase | |||||||||||||||
![]() | STRUCTURAL PROTEIN / acylphosphatase | |||||||||||||||
Function / homology | acylphosphatase / Acylphosphatase signature 1. / Acylphosphatase, conserved site / acylphosphatase activity / Acylphosphatase / Acylphosphatase-like domain / Acylphosphatase-like domain profile. / Acylphosphatase-like domain superfamily / Acylphosphatase![]() | |||||||||||||||
Biological species | ![]() ![]() | |||||||||||||||
Method | ![]() ![]() ![]() | |||||||||||||||
![]() | Lee, K.-Y. / Kim, D.-G. / Lee, B.-J. | |||||||||||||||
Funding support | ![]()
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![]() | ![]() Title: acylphosphatase from Staphylococcus aureus Authors: Lee, K.-Y. | |||||||||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 90.8 KB | Display | ![]() |
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PDB format | ![]() | 68.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 435.9 KB | Display | ![]() |
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Full document | ![]() | 437.4 KB | Display | |
Data in XML | ![]() | 10 KB | Display | |
Data in CIF | ![]() | 13.2 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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2 | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 12205.601 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Gene: acyP, yccX, BN1321_260044, BTN44_05560, DDL17_12795, DQV20_10240, DQV53_07555, E4U00_04725, EP54_14800, EQ90_12880, ERS072840_02314, FA040_08725, FVP29_18130, GIX97_03140, GO677_08310, GO706_ ...Gene: acyP, yccX, BN1321_260044, BTN44_05560, DDL17_12795, DQV20_10240, DQV53_07555, E4U00_04725, EP54_14800, EQ90_12880, ERS072840_02314, FA040_08725, FVP29_18130, GIX97_03140, GO677_08310, GO706_12140, GO746_10695, GO793_05135, GO803_14910, GO805_11030, GO810_04440, GO894_09605, GO941_00230, HMPREF3211_00435, M1K003_0247, NCTC10654_01455, NCTC10702_02217, NCTC5664_03214, NCTC6133_01806, NCTC7878_01640, NCTC9944_01419, RK64_07545, SAMEA1469856_01199, SAMEA1469884_02272, SAMEA1531680_02336, SAMEA1531701_02465, SAMEA2080329_01054, SAMEA2080330_01500, SAMEA2080334_01727, SAMEA2080433_01274, SAST44_01480, SAST45_01515 Production host: ![]() ![]() #2: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.15 Å3/Da / Density % sol: 42.83 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, sitting drop Details: 100 mM Tris, pH 8.5, 30% (w/v) PEG4000, 200 mM Sodium acetate |
-Data collection
Diffraction | Mean temperature: 100 K / Serial crystal experiment: N |
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Diffraction source | Source: ![]() ![]() |
Detector | Type: ADSC QUANTUM 270 / Detector: CCD / Date: May 25, 2014 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9794 Å / Relative weight: 1 |
Reflection | Resolution: 1.49→30 Å / Num. obs: 32259 / % possible obs: 94.1 % / Redundancy: 3.5 % / CC1/2: 0.984 / Net I/σ(I): 26.94 |
Reflection shell | Resolution: 1.49→1.52 Å / Num. unique obs: 1417 / CC1/2: 0.901 |
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Processing
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Refinement | Method to determine structure: ![]() Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS U VALUES : REFINED INDIVIDUALLY
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso max: 73.68 Å2 / Biso mean: 22.39 Å2 / Biso min: 13.86 Å2
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Refinement step | Cycle: final / Resolution: 1.49→25.72 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.493→1.532 Å / Rfactor Rfree error: 0 / Total num. of bins used: 20
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