SASDDQ7

p-hydroxyphenylacetate 3-hydroxylase, reductase component (mutant): 8 mg/ml of E248A/E251A C1 in the absence of p-hydroxyphenylacetic acid (HPA)

Data type: SASBDB experimental data Status: Published Curve type: Single concentration Last updated: 2019-12-06T13:07:15.624532+01:00

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1. Samples, Components and Experimental Conditions Sample & Experiment

Sample 1 · p-hydroxyphenylacetate 3-hydroxylase, reductase component (mutant): 8 mg/ml of E248A/E251A C1 in the absence of p-hydroxyphenylacetic acid (HPA)

Concentration	— – 8.0	Buffer / pH	50 mM MOPS, 0.5 mM EDTA, 1 mM DTT, 50 mM NaCl, and 5% glycerol / 7.0
Experimental temperature	16.0	Facility / beamline	Synchrotron Light Research Institute (SLRI) / BL1.3W
Wavelength	0.13776 nm	Exposure	600.0 s × 1

Molecular Components

Component	Type / organism	UniProt and Construct	Oligomeric State	Molecular weight
p-hydroxyphenylacetate 3-hydroxylase (HPAH), reductase component E248A/E251A C1 View sequence >GI\|45685345\|GB\|AAS75430.1\|P-HYDROXYPHENYLACETATEHYDROXYLASEC1:REDUCTASECOMPONENT[ACINETOBACTERBAUMANNII]MNQLNTAIVEKEVIDPMAFRRALGNFATGVTIMTAQTSSGERVGVTANSFNSVSLDPALVLWSIDKKSSSYRIFEEATHFGVNILSAAQIELSNRFARRSEDKFANIEFDLGVGNIPLFKNCSAAFECERYNIVEGGDHWIIIGRVVKFHDHGRSPLLYHQGAYSAVLPHPSLNMKSETAEGVFPGRLYDNMYYLLTQAVRAYQNDYQPKQLASGFRTSEARLLLVLESKTASSKCDLQREVAMPIRAIEAATKILSEKGLLIDNGQHYELTEQGNACAHMLYKIAESHQEEVFAKYTVDERKLFKNMLKDLIGI	proteinAcinetobacter baumannii	Q6Q271—–—	dimerMolecule count 2	35.296 kDa

Experimental Curves

Curve	Points / columns	q range	Uncertainty quality	Negative-intensity points	Source file
1	907[3]	0.0298341958–0.275187577 1/A	Has uncertainty columnMissing 0	0	sasbdb/entries/q7/sasddq7/source/SASDDQ7.dat

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2. Measurements Reported by SASBDB Reported Results

Metric	Method	Value	Uncertainty	Unit
dmax	P(r)	7.05	—	Å
i0	Guinier	243.28	0.34	arbitrary
i0	P(r)	254.3	—	arbitrary
mw	Experimental	65.0	—	kDa
porod_volume	Porod	95.0	—	Å³
rg	Guinier	2.397	0.004	Å
rg	P(r)	2.49	—	Å

These values are reported by SASBDB; SAXSdb did not recalculate them from the experimental curve.

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3. Source Fits and Models Source Fits & Models

This entry has no source fit record.

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4. Source File Index Source Files

Category	Path	Download status	Size
curve	sasbdb/entries/q7/sasddq7/source/SASDDQ7.dat	downloaded	43394
full_entry_zip	sasbdb/entries/q7/sasddq7/source/SASDDQ7.zip	downloaded	36645
pddf	sasbdb/entries/q7/sasddq7/source/SASDDQ7.out	downloaded	81784
sascif	sasbdb/entries/q7/sasddq7/source/SASDDQ7.sascif	downloaded	102213
summary	sasbdb/entries/q7/sasddq7/source/summary.json	downloaded	6411

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5. Experiment Description and Publication Experiment & Publication

▼

6. Complete Source Record Complete Source Record

The following content comes directly from the SASBDB entry. Missing values are shown as “—”; SAXSdb does not infer undeclared units.

Open the original SASBDB entry

Buffer and Sample Properties

Buffer name	50 mM MOPS, 0.5 mM EDTA, 1 mM DTT, 50 mM NaCl, and 5% glycerol	Buffer concentration	—
pH	7.0	Additives	—
Buffer description	—
Purity measurement method	—	Extinction coefficient	—
Absorbance	—	Scattering contrast	—
Specific volume / dry volume	— / —	Mixture / deuteration	— / —

Acquisition Conditions and Instrument

Measurement date	2018-05-26	Storage / measurement temperature	4.0 / 16.0
Exposure time	600.0	Frames	1
Wavelength	0.13776	Sample-to-detector distance	1.332
Source	X-ray synchrotron	Detector	Rayonix SX165
Facility / beamline	Synchrotron Light Research Institute (SLRI) / BL1.3W · Nakhon Ratchasima, Thailand
q range	0.298 – 2.752	Sample volume / flow rate	— / —

Original SASBDB Plots

Downloadable Files

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full_entry_zip：source record and ZIP contents (2 items)

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pddf：source record

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sascif：source record

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summary：source record

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All source fields (unfiltered)

Every source field is expanded here, including empty values, list members and fields already shown above.

summary.json：134 field values

Field path	Raw value
code	SASDDQ7
status	Published
type_of_curve	Single concentration
angular_unit	1/A
project.title	Crystal structure of the flavin reductase of Acinetobacter baumannii p-hydroxyphenylacetate 3-hydroxylase (HPAH) and identification of amino acid residues underlying its regulation by aromatic ligands.
project.publication.title	Crystal structure of the flavin reductase of Acinetobacter baumannii p-hydroxyphenylacetate 3-hydroxylase (HPAH) and identification of amino acid residues underlying its regulation by aromatic ligands.
project.publication.author_list	Yuenyao A, Petchyam N, Kamonsutthipaijit N, Chaiyen P, Pakotiprapha D
project.publication.journal	Arch Biochem Biophys
project.publication.doi	10.1016/j.abb.2018.06.010
project.publication.pmid	29940152
project.publication.published_date	2018 Sep 1
project.status	released
project.submitted_date	2018-06-05
project.released_date	2018-06-29
pddf_data	https://www.sasbdb.org/media/p_of_R_files/SASDDQ7.out
intensities_data	https://www.sasbdb.org/media/intensities_files/SASDDQ7.dat
intensities_log_plot	https://www.sasbdb.org/media/intensities_files/scattering_plots/SASDDQ7_dat_img.png
intensities_kratky_plot	https://www.sasbdb.org/media/intensities_files/scattering_plots/SASDDQ7_kratky_img.png
pddf_plot	https://www.sasbdb.org/media/p_of_R_files/pofr_images/SASDDQ7_pofr_img.png
intensities_guinier_plot	https://www.sasbdb.org/media/intensities_files/scattering_plots/SASDDQ7_guinier_img.png
sascif_data	https://www.sasbdb.org/media/sascif/sascif_files/SASDDQ7.sascif
experiment.instrument.detector.type	CCD
experiment.instrument.detector.name	Rayonix SX165
experiment.instrument.detector.resolution	15.0
experiment.instrument.name	Synchrotron Light Research Institute (SLRI)
experiment.instrument.city	Nakhon Ratchasima
experiment.instrument.country	Thailand
experiment.instrument.beamline_name	BL1.3W
experiment.instrument.beam_geometry	null
experiment.instrument.type_of_source	X-ray synchrotron
experiment.instrument.point_source	null
experiment.instrument.line_collimation	null
experiment.instrument.sample_path_length	null
experiment.instrument.line_collimation_slitlength	null
experiment.instrument.line_collimation_integrationwidth	null
experiment.instrument.xray_energy	null
experiment.instrument.beam_profile_ah	null
experiment.instrument.beam_profile_al	null
experiment.sample.molecule[0].long_name	p-hydroxyphenylacetate 3-hydroxylase (HPAH), reductase component E248A/E251A C1
experiment.sample.molecule[0].short_name	E248A/E251A C1
experiment.sample.molecule[0].sequence	>gi\|45685345\|gb\|AAS75430.1\| p-hydroxyphenylacetate hydroxylase C1:reductase component [Acinetobacter baumannii] MNQLNTAIVEKEVIDPMAFRRALGNFATGVTIMTAQTSSGERVGVTANSFNSVSLDPALVLWSIDKKSSS YRIFEEATHFGVNILSAAQIELSNRFARRSEDKFANIEFDLGVGNIPLFKNCSAAFECERYNIVEGGDHW IIIGRVVKFHDHGRSPLLYHQGAYSAVLPHPSLNMKSETAEGVFPGRLYDNMYYLLTQAVRAYQNDYQPK QLASGFRTSEARLLLVLESKTASSKCDLQREVAMPIRAIEAATKILSEKGLLIDNGQHYELTEQGNACAH MLYKIAESHQEEVFAKYTVDERKLFKNMLKDLIGI
experiment.sample.molecule[0].organism	Acinetobacter baumannii
experiment.sample.molecule[0].uniprot_code	Q6Q271
experiment.sample.molecule[0].uniprot_range_first	null
experiment.sample.molecule[0].uniprot_range_last	null
experiment.sample.molecule[0].oligomerization	dimer
experiment.sample.molecule[0].molecular_type	protein
experiment.sample.molecule[0].uniprot_sequence	MNQLNTAIVEKEVIDPMAFRRALGNFATGVTIMTAQTSSGERVGVTANSFNSVSLDPALV LWSIDKKSSSYRIFEEATHFGVNILSAAQIELSNRFARRSEDKFANIEFDLGVGNIPLFK NCSAAFECERYNIVEGGDHWIIIGRVVKFHDHGRSPLLYHQGAYSAVLPHPSLNMKSETA EGVFPGRLYDNMYYLLTQAVRAYQNDYQPKQLASGFRTSEARLLLVLESKTASSKCDLQR EVAMPIREIEEATKILSEKGLLIDNGQHYELTEQGNACAHMLYKIAESHQEEVFAKYTVD ERKLFKNMLKDLIGI
experiment.sample.molecule[0].mw	35.296
experiment.sample.molecule[0].total_mw	70.592
experiment.sample.molecule[0].number_molecules	2
experiment.sample.molecule[0].complex_state	False
experiment.sample.molecule[0].deuteration	null
experiment.sample.molecule[0].molecule_source	biological
experiment.sample.molecule[0].molecule_description	null
experiment.sample.buffer.name	50 mM MOPS, 0.5 mM EDTA, 1 mM DTT, 50 mM NaCl, and 5% glycerol
experiment.sample.buffer.concentration_unit	null
experiment.sample.buffer.comment	null
experiment.sample.buffer.additive	null
experiment.sample.buffer.concentration	null
experiment.sample.buffer.pka	null
experiment.sample.buffer.ph	7.0
experiment.sample.buffer.deuteration	null
experiment.sample.purity_method	null
experiment.sample.name	p-hydroxyphenylacetate 3-hydroxylase, reductase component (mutant): 8 mg/ml of E248A/E251A C1 in the absence of p-hydroxyphenylacetic acid (HPA)
experiment.sample.ext_coefficient	null
experiment.sample.contrast	null
experiment.sample.specific_vol	null
experiment.sample.dry_vol	null
experiment.sample.absorbption	null
experiment.sample.deuteration	null
experiment.sample.mixture	null
experiment.contributor[0].affiliation[0].short_name	null
experiment.contributor[0].affiliation[0].address	Thailand
experiment.contributor[0].affiliation[0].full_name	Mahidol University
experiment.contributor[0].affiliation[0].webpage	https://mahidol.ac.th/
experiment.contributor[0].contributor_name	Anan
experiment.contributor[0].contributor_surname	Yuenyao
experiment.contributor[0].orcid	null
experiment.concentration_method	null
experiment.concentration_unit	null
experiment.date	2018-05-26
experiment.storage_temperature	4.0
experiment.cell_temperature	16.0
experiment.exposure_time	600.0
experiment.number_of_frames	1
experiment.wavelength	0.13776
experiment.sample_detector_distance	1.332
experiment.concentration_min	null
experiment.concentration_max	8.0
experiment.sample_volume	null
experiment.flow_rate	null
experiment.s_min	0.298
experiment.s_max	2.752
experiment.total_exposure_time	null
experiment.seccolumn	null
fits	[]
estimated_volume_method	null
pddf_software	ATSAS GNOM
pddf_software_version	5.0
i0_calibration_standard	null
description	null
experiment_description	null
tags	[]
intensity_unit	arbitrary
experimental_mw	65.0
experimental_mw_error	null
guinier_i0_mw	null
guinier_i0_mw_error	null
porod_mw	null
porod_mw_error	null
pddf_i0	254.3
pddf_i0_error	null
guinier_i0	243.28
guinier_i0_error	0.34
pddf_rg	2.49
pddf_rg_error	null
guinier_rg	2.397
guinier_rg_error	0.004
pddf_dmax	7.05
pddf_dmax_error	null
porod_volume	95.0
porod_volume_error	null
estimated_volume	null
estimated_volume_error	null
guinier_point_first	24
guinier_point_last	89
pddf_point_first	null
pddf_point_last	null
i0_calibration_standard_data	null
intensities_log_log_plot	SASDDQ7_datloglog_img.png
symmetry	null
last_modified	2019-12-06T13:07:15.624532+01:00
bragg_peak	[]

manifest.json：36 field values

Field path	Raw value
code	SASDDQ7
status	success
started_at	2026-08-11T15:36:25.694782+00:00
finished_at	2026-08-11T15:36:35.610268+00:00
source_last_modified	2019-12-06T13:07:15.624532+01:00
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View the complete summary.json source

{
  "code": "SASDDQ7",
  "status": "Published",
  "type_of_curve": "Single concentration",
  "angular_unit": "1/A",
  "project": {
    "title": "Crystal structure of the flavin reductase of Acinetobacter baumannii p-hydroxyphenylacetate 3-hydroxylase (HPAH) and identification of amino acid residues underlying its regulation by aromatic ligands.",
    "publication": {
      "title": "Crystal structure of the flavin reductase of Acinetobacter baumannii p-hydroxyphenylacetate 3-hydroxylase (HPAH) and identification of amino acid residues underlying its regulation by aromatic ligands.",
      "author_list": "Yuenyao A, Petchyam N, Kamonsutthipaijit N, Chaiyen P, Pakotiprapha D",
      "journal": "Arch Biochem Biophys",
      "doi": "10.1016/j.abb.2018.06.010",
      "pmid": "29940152",
      "published_date": "2018 Sep 1"
    },
    "status": "released",
    "submitted_date": "2018-06-05",
    "released_date": "2018-06-29"
  },
  "pddf_data": "https://www.sasbdb.org/media/p_of_R_files/SASDDQ7.out",
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        "name": "Rayonix SX165",
        "resolution": 15.0
      },
      "name": "Synchrotron Light Research Institute (SLRI)",
      "city": "Nakhon Ratchasima",
      "country": "Thailand",
      "beamline_name": "BL1.3W",
      "beam_geometry": null,
      "type_of_source": "X-ray synchrotron",
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    },
    "sample": {
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        {
          "long_name": "p-hydroxyphenylacetate 3-hydroxylase (HPAH), reductase component E248A/E251A C1",
          "short_name": "E248A/E251A C1",
          "sequence": ">gi|45685345|gb|AAS75430.1| p-hydroxyphenylacetate hydroxylase C1:reductase component [Acinetobacter baumannii]\r\nMNQLNTAIVEKEVIDPMAFRRALGNFATGVTIMTAQTSSGERVGVTANSFNSVSLDPALVLWSIDKKSSS\r\nYRIFEEATHFGVNILSAAQIELSNRFARRSEDKFANIEFDLGVGNIPLFKNCSAAFECERYNIVEGGDHW\r\nIIIGRVVKFHDHGRSPLLYHQGAYSAVLPHPSLNMKSETAEGVFPGRLYDNMYYLLTQAVRAYQNDYQPK\r\nQLASGFRTSEARLLLVLESKTASSKCDLQREVAMPIRAIEAATKILSEKGLLIDNGQHYELTEQGNACAH\r\nMLYKIAESHQEEVFAKYTVDERKLFKNMLKDLIGI",
          "organism": "Acinetobacter baumannii",
          "uniprot_code": "Q6Q271",
          "uniprot_range_first": null,
          "uniprot_range_last": null,
          "oligomerization": "dimer",
          "molecular_type": "protein",
          "uniprot_sequence": "MNQLNTAIVEKEVIDPMAFRRALGNFATGVTIMTAQTSSGERVGVTANSFNSVSLDPALV\nLWSIDKKSSSYRIFEEATHFGVNILSAAQIELSNRFARRSEDKFANIEFDLGVGNIPLFK\nNCSAAFECERYNIVEGGDHWIIIGRVVKFHDHGRSPLLYHQGAYSAVLPHPSLNMKSETA\nEGVFPGRLYDNMYYLLTQAVRAYQNDYQPKQLASGFRTSEARLLLVLESKTASSKCDLQR\nEVAMPIREIEEATKILSEKGLLIDNGQHYELTEQGNACAHMLYKIAESHQEEVFAKYTVD\nERKLFKNMLKDLIGI",
          "mw": 35.296,
          "total_mw": 70.592,
          "number_molecules": 2,
          "complex_state": false,
          "deuteration": null,
          "molecule_source": "biological",
          "molecule_description": null
        }
      ],
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        "concentration_unit": null,
        "comment": null,
        "additive": null,
        "concentration": null,
        "pka": null,
        "ph": 7.0,
        "deuteration": null
      },
      "purity_method": null,
      "name": "p-hydroxyphenylacetate 3-hydroxylase, reductase component (mutant): 8 mg/ml of E248A/E251A C1 in the absence of p-hydroxyphenylacetic acid (HPA)",
      "ext_coefficient": null,
      "contrast": null,
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Title	Crystal structure of the flavin reductase of Acinetobacter baumannii p-hydroxyphenylacetate 3-hydroxylase (HPAH) and identification of amino acid residues underlying its regulation by aromatic ligands.
Authors	Yuenyao A, Petchyam N, Kamonsutthipaijit N, Chaiyen P, Pakotiprapha D
DOI / PMID	10.1016/j.abb.2018.06.010 / 29940152