4I6M: Actin-related protein 7

Structure of Arp7-Arp9-Snf2(HSA)-RTT102 subcomplex of SWI/SNF chromatin remodeler. Determined by X-ray diffraction at 2.8 Å resolution. Released 13 Feb 2013.

Method: X-ray diffraction
Resolution: 2.8 Å
Organism: Saccharomyces cerevisiae
Chains: 4
Atoms: 7,660
Mol. weight: 136.73 kDa
Ligands: PO4
Released: 13 Feb 2013

Explore 4I6M in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4I6M contains 48 α-helices and 43 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: 24 helices, 19 β-strands

Element	Residues	Length	Sheet
β-strand	8-12	5	1
β-strand	16-21	6	1
β-strand	29-32	4	1
β-strand	34-37	4	2
β-strand	47-48	2	2
α-helix	51-59	9
β-strand	66-69	4	2
β-strand	71	1	3
β-strand	77	1	3
α-helix	80-93	14
β-strand	104-108	5	1
α-helix	116-124	9
α-helix	125-130	6
β-strand	135-140	6	1
α-helix	141-147	7
β-strand	154-159	6	4
β-strand	164-170	7	4
β-strand	173-174	2	4
α-helix	176-178	3
β-strand	180-181	2	4
α-helix	186-197	12
α-helix	198-200	3
α-helix	217-225	9
α-helix	227-234	8
α-helix	243-261	19
α-helix	283-285	3
β-strand	287-292	6	5
α-helix	293-295	3
β-strand	297-302	6	5
α-helix	303-314	12
α-helix	316-318	3
α-helix	325-327	3
α-helix	329-338	10
α-helix	381-388	8
β-strand	392-395	4	4
α-helix	397-400	4
α-helix	404-415	12
β-strand	423-424	2	4
α-helix	429-433	5
α-helix	435-444	10
α-helix	449-451	3
β-strand	454-456	3	1
α-helix	457-463	7

Chain B: 21 helices, 19 β-strands

Element	Residues	Length	Sheet
α-helix	6-8	3
β-strand	10-14	5	6
β-strand	18-23	6	6
α-helix	30-33	4
β-strand	35-38	4	6
β-strand	41-45	5	7
β-strand	51-54	4	7
α-helix	58-60	3
β-strand	63-65	3	7
β-strand	68-69	2	8
β-strand	72-73	2	8
α-helix	76-98	23
β-strand	111-115	5	6
α-helix	121-133	13
β-strand	139-144	6	6
α-helix	145-152	8
β-strand	159-164	6	9
β-strand	169-175	7	9
β-strand	178-179	2	9
β-strand	185-187	3	9
α-helix	191-201	11
α-helix	207-214	8
α-helix	276-278	3
β-strand	282-285	4	10
β-strand	291-294	4	10
α-helix	296-299	4
α-helix	303-317	15
α-helix	323-329	7
β-strand	333-336	4	9
α-helix	338-341	4
α-helix	345-357	13
α-helix	363-372	10
α-helix	396-400	5
β-strand	409	1	9
α-helix	410-413	4
α-helix	417-422	6
α-helix	428-440	13
β-strand	449-450	2	6
α-helix	451-457	7
α-helix	458-464	7

Chain C: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	593-657	65

Chain D: 2 helices, 5 β-strands

Element	Residues	Length	Sheet
α-helix	3-9	7
β-strand	25-30	6	11
β-strand	33	1	12
β-strand	55	1	12
β-strand	60-65	6	11
α-helix	66-67	2
β-strand	88	1	6

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Actin-related protein 7	A	protein	477	Saccharomyces cerevisiae	Q12406 (AlphaFold model)
Actin-like protein ARP9	B	protein	439	Saccharomyces cerevisiae	Q05123 (AlphaFold model)
Actin-like protein ARP9	C	protein	106	Saccharomyces cerevisiae	P22082 (AlphaFold model)
Regulator of Ty1 transposition protein 102	D	protein	157	Saccharomyces cerevisiae	P53330 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>4I6M_1 Actin-related protein 7 (chains A)
MTLNRKCVVIHNGSHRTVAGFSNVELPQCIIPSSYIKRTDEGGEAEFIFGTYNMIDAAAE
KRNGDEVYTLVDSQGLPYNWDALEMQWRYLYDTQLKVSPEELPLVITMPATNGKPDMAIL
ERYYELAFDKLNVPVFQIVIEPLAIALSMGKSSAFVIDIGASGCNVTPIIDGIVVKNAVV
RSKFGGDFLDFQVHERLAPLIKEENDMENMADEQKRSTDVWYEASTWIQQFKSTMLQVSE
KDLFELERYYKEQADIYAKQQEQLKQMDQQLQYTALTGSPNNPLVQKKNFLFKPLNKTLT
LDLKECYQFAEYLFKPQLISDKFSPEDGLGPLMAKSVKKAGASINSMKANTSTNPNGLGT
SHINTNVGDNNSTASSSNISPEQVYSLLLTNVIITGSTSLIEGMEQRIIKELSIRFPQYK
LTTFANQVMMDRKIQGWLGALTMANLPSWSLGKWYSKEDYETLKRDRKQSQATNATN

Sequence of entity 2 (B), FASTA

>4I6M_2 Actin-like protein ARP9 (chains B)
MAPFRQDSILIIYPRSQTTLVQFGLNEETFTVPELEIPTQIYRTTRQDGSYTYHSTNKDN
KAELIKPIQNGEIIDISAFTQFLRLIFVSILSDRANKNQDAFEAELSNIPLLLITHHSWS
QSDLEIITQYVFESLEINNLIQLPASLAATYSMISLQNCCIIDVGTHHTDIIPIVDYAQL
DHLVSSIPMGGQSINDSLKKLLPQWDDDQIESLKKSPIFEVLSDDAKKLSSFDFGNENED
EDEGTLKNSDLEFNTFWDEKGNEIKVGKQRFQGCNNLIKNISNRVGLTLDNIDDINKAKA
VWENIIIVGGTTSISGFKEALLGQLLKDHLIIEPEEEKSKREEEAKSVLPAATKKKSKFM
TNSTAFVPTIEYVQCPTVIKLAKYPDYFPEWKKSGYSEIIFLGAQIVSKQIFTHPKDTFY
ITREKYNMKGPAALWDVQF

Sequence of entity 3 (C), FASTA

>4I6M_3 Actin-like protein ARP9 (chains C)
MGHHHHHHHHHHGNVQDALLTNQLYKNHELLKLERKKTEAVARLKSMNKSAINQYNRRQD
KKNKRLKFGHRLIATHTNLERDEQKRAEKKAKERLQALKANDEEAY

Sequence of entity 4 (D), FASTA

>4I6M_4 Regulator of Ty1 transposition protein 102 (chains D)
MDPQTLITKANKVSYYGNPTSKESWRYDWYQPSKVSSNVQQPQQQLGDMENNLEKYPFRY
KTWLRNQEDEKNLQRESCEDILDLKEFDRRILKKSLMTSHTKGDTSKATGAPSANQGDEA
LSVDDIRGAVGNSEAIPGLSAGVNNDNTKESKDVKMN

Ligands and cofactors

ID	Name	Formula	Copies
PO4	Phosphate ion	O4 P	12

Primary citation

Structure of an actin-related subcomplex of the SWI/SNF chromatin remodeler. Schubert, H.L., Wittmeyer, J., Kasten, M.M. et al. Proc Natl Acad Sci U S A (2013) 110:3345-3350. DOI 10.1073/pnas.1215379110 · PubMed

Other PDB entries of the same protein (UniProt Q12406 (AlphaFold model), which also has an AlphaFold model), best resolution first:

7C4J 2.89 Å, Cryo-EM structure of the yeast Swi/Snf complex in a nucleosome free state
3WEE 3.1 Å, Structure of the full-length yeast Arp7-Arp9 Heterodimer
5TGC 3.25 Å, Structure of the hetero-trimer of Rtt102-Arp7/9 bound to ATP
6VZ4 3.9 Å, Cryo-EM structure of Sth1-Arp7-Arp9-Rtt102 bound to the nucleosome in ADP Beryllium…
9PB3 4.0 Å, ARP of SWI/SNF of PIC-Med-SWI/SNF
6VZG 4.2 Å, Cryo-EM structure of Sth1-Arp7-Arp9-Rtt102
7EGP 6.9 Å, The structure of SWI/SNF-nucleosome complex
6KW3 7.13 Å, The ClassA RSC-Nucleosome Complex
6KW4 7.55 Å, The ClassB RSC-Nucleosome Complex
6UXW 8.96 Å, SWI/SNF nucleosome complex with ADP-BeFx
6KW5 10.13 Å, The ClassC RSC-Nucleosome Complex
6TDA 15.0 Å, Structure of SWI/SNF chromatin remodeler RSC bound to a nucleosome

Browse structure collections

About this viewer

MolViewer shows 4I6M directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.