3MP8: Sgf29 tudor domain

Crystal structure of Sgf29 tudor domain. Determined by X-ray diffraction at 1.92 Å resolution. Released 4 May 2011.

Method
X-ray diffraction
Resolution
1.92 Å
Organisms
Escherichia coli K-12, unidentified, Saccharomyces cerevisiae S288C
Chains
1
Atoms
4,591
Mol. weight
59.71 kDa
Ligands
4BZ
Released
4 May 2011

Explore 3MP8 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3MP8 contains 31 α-helices and 36 β-strands across 1 chain. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 31 helices, 36 β-strands

ElementResiduesLengthSheet
β-strand745-74841
α-helix755-76915
β-strand773-77641
α-helix781-7899
β-strand797-80151
α-helix802-8043
α-helix805-8106
β-strand81412
α-helix815-8173
α-helix821-8244
β-strand82713
α-helix829-8346
β-strand836-83724
β-strand840-84124
β-strand844-84961
β-strand852-85655
β-strand86616
α-helix867-8693
α-helix870-8789
β-strand883-88535
α-helix892-8943
α-helix896-9016
β-strand905-91067
β-strand913-92087
α-helix924-93815
α-helix948-9569
β-strand960-96565
α-helix967-9693
α-helix970-9767
β-strand980-98345
α-helix984-9863
β-strand98716
β-strand98818
β-strand99118
α-helix9951
β-strand996-99729
β-strand998-100471
β-strand100512
α-helix1011-10177
α-helix1018-10225
α-helix1025-103410
β-strand1039-104021
β-strand104213
α-helix1043-10497
α-helix1053-106412
β-strand1066-106729
α-helix1068-10692
α-helix1074-109017
α-helix1095-110511
β-strand1111110
β-strand1125110
β-strand1130-1133411
β-strand1144-11531011
β-strand1158-1163611
β-strand1174-1179611
α-helix1180-11823
β-strand1183-1185311
α-helix1186-11872
α-helix1194-11963
β-strand1200-1204511
α-helix12051
β-strand1210-12191011
α-helix12241
β-strand1225-1229511
β-strand1239-1241311
α-helix1243-12453
β-strand1246-1248311

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Maltose-binding periplasmic protein,LINKER,SAGA-associated factor 29Aprotein522Escherichia coli K-12, unidentified, Saccharomyces cerevisiae S288CP0AEX9 (AlphaFold model), P25554 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>3MP8_1 Maltose-binding periplasmic protein,LINKER,SAGA-associated factor 29 (chains A)
MKIEEGKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGPDI
IFWAHDRFGGYAQSGLLAEITPDKAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNK
DLLPNPPKTWEEIPALDKELKAKGKSALMFNLQEPYFTWPLIAADGGYAFKYENGKYDIK
DVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDTSK
VNYGVTVLPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLEAVNKDKPL
GAVALKSYEEELAKDPRIAATMENAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVDE
ALAAAQTNAAAEFGSSYWTSEYNPNAPILVGSEVAYKPRRGSADGEWIQCEVLKVVADGT
RFEVRDPEPDELGNSGKVYKCNRKELLLIPPGFPTKNYPPGTKVLARYPETTTFYPAIVI
GTKRDGTCRLRFDGEEEVDKETEVTRRLVLPSPTALANLARK

Ligands and cofactors

IDNameFormulaCopies
4BZ4-(hydroxymethyl)benzamidineC8 H10 N2 O1

Water and common crystallization additives (ACY, NA, SO4, GOL) are not listed.

Primary citation

Sgf29 binds histone H3K4me2/3 and is required for SAGA complex recruitment and histone H3 acetylation. Bian, C., Xu, C., Ruan, J. et al. EMBO J (2011) 30:2829-2842. DOI 10.1038/emboj.2011.193 · PubMed

Other PDB entries of the same protein (UniProt P0AEX9 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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