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Structure paper

TitleStructural studies of human histone deacetylase 8 and its site-specific variants complexed with substrate and inhibitors.
Journal, issue, pagesBiochemistry, Vol. 47, Page 13554-13563, Year 2008
Publish dateOct 14, 2008 (structure data deposition date)
AuthorsDowling, D.P. / Gantt, S.L. / Gattis, S.G. / Fierke, C.A. / Christianson, D.W.
External linksBiochemistry / PubMed:19053282
MethodsX-ray diffraction
Resolution1.8 - 3.3 Å
Structure data

PDB-3ew8:
Crystal Structure Analysis of human HDAC8 D101L variant
Method: X-RAY DIFFRACTION / Resolution: 1.8 Å

PDB-3ewf:
Crystal Structure Analysis of human HDAC8 H143A variant complexed with substrate.
Method: X-RAY DIFFRACTION / Resolution: 2.5 Å

PDB-3ezp:
Crystal Structure Analysis of human HDAC8 D101N variant
Method: X-RAY DIFFRACTION / Resolution: 2.65 Å

PDB-3ezt:
Crystal Structure Analysis of Human HDAC8 D101E Variant
Method: X-RAY DIFFRACTION / Resolution: 2.85 Å

PDB-3f06:
Crystal Structure Analysis of Human HDAC8 D101A Variant.
Method: X-RAY DIFFRACTION / Resolution: 2.55 Å

PDB-3f07:
Crystal Structure Analysis of Human HDAC8 complexed with APHA in a new monoclinic crystal form
Method: X-RAY DIFFRACTION / Resolution: 3.3 Å

PDB-3f0r:
Crystal Structure Analysis of Human HDAC8 complexed with trichostatin A in a new monoclinic crystal form
Method: X-RAY DIFFRACTION / Resolution: 2.54 Å

Chemicals

ChemComp-K:
Unknown entry

ChemComp-ZN:
Unknown entry

ChemComp-B3N:
4-(dimethylamino)-N-[7-(hydroxyamino)-7-oxoheptyl]benzamide

ChemComp-BME:
BETA-MERCAPTOETHANOL

ChemComp-GOL:
GLYCEROL

ChemComp-HOH:
WATER

ChemComp-MCM:
7-AMINO-4-METHYL-CHROMEN-2-ONE

ChemComp-AGE:
(2E)-N-hydroxy-3-[1-methyl-4-(phenylacetyl)-1H-pyrrol-2-yl]prop-2-enamide

ChemComp-TSN:
TRICHOSTATIN A

Source
  • homo sapiens (human)
  • synthetic construct (others)
KeywordsHYDROLASE / HDAC / metalloenzyme / arginase fold / HDAC8 / histone deacetylase / hydroxamate inhibitor / unliganded / Chromatin regulator / Nucleus / Repressor / Transcription / Transcription regulation / acetylation / substrate complex / Alternative splicing / histone deacetylase 8 / mutant

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