3MEU: SGF29

Crystal structure of SGF29 in complex with H3R2me2sK4me3. Determined by X-ray diffraction at 1.28 Å resolution. Released 28 Apr 2010.

Method: X-ray diffraction
Resolution: 1.28 Å
Organisms: Homo sapiens, Xenopus laevis
Chains: 4
Atoms: 3,336
Mol. weight: 44.08 kDa
Released: 28 Apr 2010

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

Secondary structure: helices and β-sheets

3MEU contains 31 α-helices and 34 β-strands across 2 chains. 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: 15 helices, 17 β-strands

Element	Residues	Length	Sheet
α-helix	115-129	15
α-helix	130-131	2
β-strand	132	1	1
α-helix	133	1
α-helix	139-142	4
β-strand	145	1	2
α-helix	148-151	4
β-strand	152	1	3
α-helix	156-157	2
β-strand	161-167	7	4
β-strand	173-184	12	4
β-strand	189-194	6	4
α-helix	202	1
β-strand	203-206	4	4
α-helix	207-209	3
β-strand	210-212	3	4
α-helix	213-214	2
β-strand	216	1	2
β-strand	217	1	1
α-helix	224-226	3
α-helix	228-229	2
β-strand	233-237	5	4
α-helix	238	1
β-strand	243-251	9	4
α-helix	258-259	2
β-strand	260-264	5	4
β-strand	265	1	5
β-strand	273	1	5
α-helix	274-276	3
β-strand	277-279	3	4
α-helix	281-283	3
β-strand	284-286	3	4

Chain B: 16 helices, 17 β-strands

Element	Residues	Length	Sheet
α-helix	117-129	13
α-helix	131	1
β-strand	132	1	6
α-helix	133	1
α-helix	141-142	2
β-strand	145	1	7
α-helix	148-150	3
β-strand	151	1	3
α-helix	156-157	2
β-strand	161-167	7	8
α-helix	168	1
β-strand	173-184	12	8
β-strand	189-194	6	8
β-strand	202-206	5	8
α-helix	207-209	3
β-strand	210-212	3	8
α-helix	213-214	2
β-strand	216	1	7
β-strand	217	1	6
α-helix	218-219	2
α-helix	224-226	3
β-strand	233-237	5	8
α-helix	238	1
β-strand	243-251	9	8
α-helix	258-259	2
β-strand	260-264	5	8
β-strand	265	1	9
β-strand	273	1	9
α-helix	274	1
α-helix	276	1
β-strand	277-279	3	8
α-helix	281-283	3
β-strand	284-286	3	8

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
SAGA-associated factor 29 homolog	A, B	protein	180	Homo sapiens	Q96ES7 (AlphaFold model)
Histone H3	C, D	protein	14	Xenopus laevis	Q92133 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>3MEU_1 SAGA-associated factor 29 homolog (chains A, B)
GRRGVLMTLLQQSAMTLPLWIGKPGDKPPPLCGAIPASGDYVARPGDKVAARVKAVDGDE
QWILAEVVSYSHATNKYEVDDIDEEGKERHTLSRRRVIPLPQWKANPETDPEALFQKEQL
VLALYPQTTCFYRALIHAPPQRPQDDYSVLFEDTSYADGYSPPLNVAQRYVVACKEPKKK

Sequence of entity 2 (C, D), FASTA

>3MEU_2 Histone H3 (chains C, D)
ARTKQTARKSTGGY

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 Q96ES7 (AlphaFold model), which also has an AlphaFold model), best resolution first:

3MEA 1.26 Å, Crystal structure of the SGF29 in complex with H3K4me3
3ME9 1.37 Å, Crystal structure of SGF29 in complex with H3K4me3 peptide
5C0M 1.6 Å, Crystal structure of SGF29 tandem tudor domain in complex with a Carba containing peptide
3LX7 1.78 Å, Crystal structure of a Novel Tudor domain-containing protein SGF29
3MEV 1.83 Å, Crystal structure of SGF29 in complex with R2AK4me3
3MEW 1.92 Å, Crystal structure of Novel Tudor domain-containing protein SGF29
3MET 2.0 Å, Crystal structure of SGF29 in complex with H3K4me2

Browse structure collections

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