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- SASDE56: Human ATP-citrate synthase (ACLY) in HBS + Citrate + Coenzyme-A -

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Basic information

Entry
Database: SASBDB / ID: SASDE56
SampleHuman ATP-citrate synthase (ACLY) in HBS + Citrate + Coenzyme-A
  • ATP-citrate synthase (protein), Homo sapiens
Function / homologyATP citrate synthase / Isoform 1 of ATP-citrate synthase
Function and homology information
Biological speciesHomo sapiens (human)
CitationDate: 2019 Apr 3
Title: Structure of ATP citrate lyase and the origin of citrate synthase in the Krebs cycle
Authors: Verschueren K / Blanchet C / Felix J / Dansercoer A / De Vos D / Bloch Y / Van Beeumen J / Svergun D / Gutsche I / Savvides S
Contact author
  • Clement Blanchet (EMBL-Hamburg, European Molecular Biology Laboratory (EMBL) - Hamburg outstation, Notkestraße 85, Geb. 25A, 22607 Hamburg, Deutschland, Germany)

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Models

Model #2506
Type: atomic / Symmetry: P222 / Chi-square value: 7.25
Search similar-shape structures of this assembly by Omokage search (details)
Model #2875
Type: atomic / Radius of dummy atoms: 1.90 A / Chi-square value: 2.75656623518009
Search similar-shape structures of this assembly by Omokage search (details)

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Sample

SampleName: Human ATP-citrate synthase (ACLY) in HBS + Citrate + Coenzyme-A
Specimen concentration: 24 mg/ml
BufferName: 20mM HEPES, 150mM NaCl, 50mM Tris, 20mM citrate, 2mM CoA
pH: 7.2
Entity #1335Type: protein / Description: ATP-citrate synthase / Formula weight: 114.58 / Num. of mol.: 4 / Source: Homo sapiens / References: UniProt: P53396-1
Sequence: MSAKAISEQT GKELLYKFIC TTSAIQNRFK YARVTPDTDW ARLLQDHPWL LSQNLVVKPD QLIKRRGKLG LVGVNLTLDG VKSWLKPRLG QEATVGKATG FLKNFLIEPF VPHSQAEEFY VCIYATREGD YVLFHHEGGV DVGDVDAKAQ KLLVGVDEKL NPEDIKKHLL ...Sequence:
MSAKAISEQT GKELLYKFIC TTSAIQNRFK YARVTPDTDW ARLLQDHPWL LSQNLVVKPD QLIKRRGKLG LVGVNLTLDG VKSWLKPRLG QEATVGKATG FLKNFLIEPF VPHSQAEEFY VCIYATREGD YVLFHHEGGV DVGDVDAKAQ KLLVGVDEKL NPEDIKKHLL VHAPEDKKEI LASFISGLFN FYEDLYFTYL EINPLVVTKD GVYVLDLAAK VDATADYICK VKWGDIEFPP PFGREAYPEE AYIADLDAKS GASLKLTLLN PKGRIWTMVA GGGASVVYSD TICDLGGVNE LANYGEYSGA PSEQQTYDYA KTILSLMTRE KHPDGKILII GGSIANFTNV AATFKGIVRA IRDYQGPLKE HEVTIFVRRG GPNYQEGLRV MGEVGKTTGI PIHVFGTETH MTAIVGMALG HRPIPGKSTT LFSRHTKAIV WGMQTRAVQG MLDFDYVCSR DEPSVAAMVY PFTGDHKQKF YWGHKEILIP VFKNMADAMR KHPEVDVLIN FASLRSAYDS TMETMNYAQI RTIAIIAEGI PEALTRKLIK KADQKGVTII GPATVGGIKP GCFKIGNTGG MLDNILASKL YRPGSVAYVS RSGGMSNELN NIISRTTDGV YEGVAIGGDR YPGSTFMDHV LRYQDTPGVK MIVVLGEIGG TEEYKICRGI KEGRLTKPIV CWCIGTCATM FSSEVQFGHA GACANQASET AVAKNQALKE AGVFVPRSFD ELGEIIQSVY EDLVANGVIV PAQEVPPPTV PMDYSWAREL GLIRKPASFM TSICDERGQE LIYAGMPITE VFKEEMGIGG VLGLLWFQKR LPKYSCQFIE MCLMVTADHG PAVSGAHNTI ICARAGKDLV SSLTSGLLTI GDRFGGALDA AAKMFSKAFD SGIIPMEFVN KMKKEGKLIM GIGHRVKSIN NPDMRVQILK DYVRQHFPAT PLLDYALEVE KITTSKKPNL ILNVDGLIGV AFVDMLRNCG SFTREEADEY IDIGALNGIF VLGRSMGFIG HYLDQKRLKQ GLYRHPWDDI SYVLPEHMSM

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Experimental information

BeamInstrument name: PETRA III EMBL P12 / City: Hamburg / 国: Germany / Type of source: X-ray synchrotronSynchrotron / Wavelength: 0.124 Å / Dist. spec. to detc.: 3.1 mm
DetectorName: Pilatus 6M
Scan
Title: Human ATP-citrate synthase (ACLY) in HBS + Citrate + CoenzymeA
Measurement date: May 5, 2018 / Storage temperature: 20 °C / Cell temperature: 20 °C / Exposure time: 1 sec. / Number of frames: 900 / Unit: 1/nm /
MinMax
Q0.0239 7.2965
Distance distribution function P(R)
Sofotware P(R): GNOM 5.0 / Number of points: 484 /
MinMax
Q0.0542511 1.38886
P(R) point1 484
R0 16.5
Result
Type of curve: sec /
ExperimentalPorod
MW480 kDa440 kDa
Volume-709 nm3

P(R)GuinierGuinier error
Forward scattering, I011900 11832 10
Radius of gyration, Rg5.768 nm5.75 nm0.01

MinMax
D-16.5
Guinier point12 74

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