4BB7: Yeast Rsc2 BAH domain

Crystal structure of the yeast Rsc2 BAH domain. Determined by X-ray diffraction at 2.4 Å resolution. Released 14 Aug 2013.

Method: X-ray diffraction
Resolution: 2.4 Å
Organism: SACCHAROMYCES CEREVISIAE
Chains: 4
Atoms: 8,175
Mol. weight: 121.56 kDa
Released: 14 Aug 2013

Explore 4BB7 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4BB7 contains 36 α-helices and 104 β-strands across 4 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: 8 helices, 26 β-strands

Element	Residues	Length	Sheet
β-strand	403-405	3	1
β-strand	408-410	3	1
β-strand	415-418	4	2
α-helix	427	1
β-strand	428-437	10	2
β-strand	443-451	9	2
α-helix	453-455	3
β-strand	458-459	2	3
β-strand	462	1	4
β-strand	463-465	3	5
β-strand	468	1	6
β-strand	470-479	10	2
α-helix	480-482	3
β-strand	483-486	4	2
β-strand	488-491	4	6
α-helix	492-497	6
β-strand	498-500	3	7
β-strand	508-511	4	6
β-strand	513-516	4	2
β-strand	521-524	4	2
α-helix	528-531	4
α-helix	534-536	3
β-strand	543-545	3	7
β-strand	549-552	4	8
β-strand	553-555	3	5
α-helix	559-561	3
α-helix	570-575	6
β-strand	576	1	9
β-strand	586	1	9
β-strand	589-590	2	3
β-strand	603	1	4
β-strand	613-614	2	8
β-strand	624-626	3	8
β-strand	631-633	3	8

Chain B: 9 helices, 26 β-strands

Element	Residues	Length	Sheet
β-strand	403-404	2	10
β-strand	409-410	2	10
β-strand	415-418	4	11
α-helix	427	1
β-strand	428-437	10	11
β-strand	443-451	9	11
α-helix	453-455	3
β-strand	457-459	3	12
β-strand	462	1	13
β-strand	464-465	2	14
β-strand	468	1	15
β-strand	470-479	10	11
α-helix	480-482	3
β-strand	483-486	4	11
β-strand	488-491	4	15
α-helix	492-497	6
β-strand	498-500	3	16
β-strand	508-511	4	15
β-strand	513-516	4	11
β-strand	521-524	4	11
α-helix	528-531	4
α-helix	534-536	3
β-strand	543-545	3	16
β-strand	549-552	4	17
β-strand	553-554	2	14
α-helix	559-561	3
α-helix	570-575	6
β-strand	576	1	18
α-helix	577	1
β-strand	586	1	18
β-strand	588-590	3	12
β-strand	603	1	13
β-strand	613-614	2	17
β-strand	624-626	3	17
β-strand	631-633	3	17

Chain C: 10 helices, 26 β-strands

Element	Residues	Length	Sheet
β-strand	403-405	3	19
β-strand	408-410	3	19
β-strand	415-418	4	20
α-helix	427	1
β-strand	428-437	10	20
β-strand	443-451	9	20
α-helix	453-455	3
β-strand	457-459	3	21
β-strand	462	1	22
β-strand	463-464	2	23
β-strand	468	1	24
β-strand	470-479	10	20
α-helix	480-482	3
β-strand	483-486	4	20
β-strand	488-491	4	24
α-helix	492-497	6
β-strand	498-500	3	25
β-strand	508-511	4	24
β-strand	513-516	4	20
β-strand	521-524	4	20
α-helix	528-531	4
α-helix	539-541	3
β-strand	543-545	3	25
β-strand	550-552	3	26
β-strand	554-555	2	23
α-helix	559-561	3
α-helix	570-572	3
α-helix	575	1
β-strand	576	1	27
α-helix	577	1
β-strand	586	1	27
β-strand	588-590	3	21
β-strand	603	1	22
β-strand	613-614	2	26
β-strand	625-626	2	26
β-strand	631-632	2	26

Chain D: 9 helices, 26 β-strands

Element	Residues	Length	Sheet
β-strand	403-405	3	28
β-strand	408-410	3	28
β-strand	415-418	4	29
α-helix	427	1
β-strand	428-437	10	29
β-strand	443-451	9	29
α-helix	453-455	3
β-strand	457-459	3	30
β-strand	462	1	31
β-strand	464	1	32
β-strand	468	1	33
β-strand	470-479	10	29
α-helix	480-482	3
β-strand	483-486	4	29
β-strand	488-491	4	33
α-helix	492-497	6
β-strand	498-500	3	34
β-strand	508-511	4	33
β-strand	513-516	4	29
β-strand	521-524	4	29
α-helix	528-531	4
α-helix	534-536	3
β-strand	543-545	3	34
β-strand	550-552	3	35
β-strand	554	1	32
α-helix	559-561	3
α-helix	570-575	6
β-strand	576	1	36
α-helix	577	1
β-strand	586	1	36
β-strand	588-590	3	30
β-strand	603	1	31
β-strand	613-614	2	35
β-strand	625-626	2	35
β-strand	631-632	2	35

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Chromatin structure-remodeling complex subunit RSC2	A, B, C, D	protein	258	SACCHAROMYCES CEREVISIAE	Q06488 (AlphaFold model)

Sequence of entity 1 (A, B, C, D), FASTA

>4BB7_1 CHROMATIN STRUCTURE-REMODELING COMPLEX SUBUNIT RSC2 (chains A, B, C, D)
MHHHHHHLEVLFQGPHMDEVIVNNISYHVGDWALLRNQNDPQKPIVGQIFRLWKTPDGKQ
WLNACWYYRPEQTVHRVDRLFYKNEVMKTGQYRDHLVSNLVGKCYVIHFTRYQRGNPDMK
LEGPLFVCEFRYNESDKIFNKIRTWKACLPEEIRDLDEATIPVNGRKFFKYPSPIRHLLP
ANATPHDRVPEPTMGSPDAPPLVGAVYMRPKMQRDDLGEYATSDDCPRYIIRPNDSPEEG
QVDIETGTITTNTPTANA

Primary citation

The Bah Domain of Rsc2 is a Histone H3 Binding Domain. Chambers, A.L., Pearl, L.H., Oliver, A.W. et al. Nucleic Acids Res (2013) 41:9168. DOI 10.1093/NAR/GKT662 · PubMed

Other PDB entries of the same protein (UniProt Q06488 (AlphaFold model), which also has an AlphaFold model), best resolution first:

6V8O 3.07 Å, RSC core
6K15 3.4 Å, RSC substrate-recruitment module
6KW3 7.13 Å, The ClassA RSC-Nucleosome Complex
6KW4 7.55 Å, The ClassB RSC-Nucleosome Complex
6KW5 10.13 Å, The ClassC RSC-Nucleosome Complex
6V92 20.0 Å, Rsc-ncp

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