4AM6: Actin-like protein ARP8

C-terminal domain of actin-related protein ARP8 from S. Cerevisiae. Determined by X-ray diffraction at 2.7 Å resolution. Released 12 Dec 2012.

Method: X-ray diffraction
Resolution: 2.7 Å
Organism: SACCHAROMYCES CEREVISIAE
Chains: 2
Atoms: 10,114
Mol. weight: 149.82 kDa
Released: 12 Dec 2012

Explore 4AM6 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4AM6 contains 71 α-helices and 55 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: 34 helices, 28 β-strands

Element	Residues	Length	Sheet
α-helix	265-267	3
β-strand	268-272	5	1
β-strand	277-281	5	1
β-strand	289-292	4	1
β-strand	295-298	4	2
α-helix	299-301	3
α-helix	321-341	21
β-strand	357-360	4	3
α-helix	361	1
β-strand	377	1	4
β-strand	384-385	2	2
α-helix	386-390	5
β-strand	392	1	4
β-strand	397-400	4	2
β-strand	403-405	3	5
β-strand	407-408	2	5
α-helix	418-433	16
β-strand	434	1	6
β-strand	439	1	6
α-helix	442-447	6
β-strand	449-454	6	1
α-helix	460-468	9
α-helix	469-473	5
β-strand	478-483	6	1
α-helix	484-491	8
β-strand	498-503	6	7
β-strand	508-514	7	7
β-strand	517-518	2	7
α-helix	520-522	3
β-strand	524-526	3	7
α-helix	530-543	14
α-helix	556-569	14
α-helix	574-576	3
β-strand	580-586	7	3
β-strand	593-600	8	3
α-helix	603-609	7
α-helix	610-612	3
α-helix	615-619	5
α-helix	622-624	3
α-helix	628-631	4
α-helix	635-637	3
β-strand	638	1	8
β-strand	645	1	8
α-helix	651-657	7
α-helix	662-664	3
α-helix	668-686	19
α-helix	703-716	14
α-helix	720-722	3
α-helix	723-727	5
β-strand	730-733	4	7
α-helix	742-753	12
β-strand	760	1	9
α-helix	763-778	16
α-helix	798-817	20
β-strand	824	1	9
β-strand	829-830	2	7
α-helix	838-840	3
α-helix	841-849	9
α-helix	853-858	6
β-strand	860-861	2	1
α-helix	862-868	7
α-helix	869-874	6

Chain B: 37 helices, 27 β-strands

Element	Residues	Length	Sheet
α-helix	265-267	3
β-strand	268-273	6	10
β-strand	277-281	5	10
β-strand	289-292	4	10
β-strand	295-298	4	11
α-helix	299-301	3
α-helix	321-341	21
α-helix	343-345	3
β-strand	377	1	12
β-strand	384-385	2	11
α-helix	386-390	5
β-strand	392	1	12
α-helix	394-396	3
β-strand	397-400	4	11
β-strand	403-404	2	13
β-strand	407-408	2	13
α-helix	418-432	15
β-strand	434-435	2	14
β-strand	438-439	2	14
α-helix	442-447	6
β-strand	449-454	6	10
α-helix	460-468	9
α-helix	469-473	5
β-strand	478-483	6	10
α-helix	484-491	8
β-strand	498-503	6	15
β-strand	508-514	7	15
β-strand	517-518	2	15
α-helix	520-522	3
β-strand	524-526	3	15
α-helix	530-542	13
α-helix	556-569	14
α-helix	574-576	3
β-strand	580-584	5	16
β-strand	596-600	5	16
α-helix	603-609	7
α-helix	610-612	3
α-helix	615-620	6
α-helix	622-624	3
α-helix	628-631	4
β-strand	638	1	17
β-strand	645	1	17
α-helix	651-658	8
α-helix	662-664	3
α-helix	668-676	9
α-helix	678-687	10
α-helix	703-717	15
α-helix	720-722	3
α-helix	723-727	5
β-strand	730-733	4	15
α-helix	742-753	12
α-helix	756-759	4
β-strand	760	1	18
α-helix	763-772	10
α-helix	776-779	4
α-helix	796-816	21
β-strand	824	1	18
β-strand	829-830	2	15
α-helix	831-832	2
α-helix	841-851	11
α-helix	853-857	5
β-strand	860-861	2	10
α-helix	862-868	7
α-helix	869-874	6

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Actin-like protein ARP8	A, B	protein	655	SACCHAROMYCES CEREVISIAE	Q12386 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>4AM6_1 ACTIN-LIKE PROTEIN ARP8 (chains A, B)
MGSSHHHHHHSSGLVPRGSHMHSEASAAPLNDEIDLNDPTATIVIHPGSNSIKIGFPKDD
HPVVVPNCVAVPKKWLDLENSEHVENVCLQREQSEEFNNIKSEMEKNFRERMRYYKRKVP
GNAHEQVVSFNENSKPEIISEKNDPSPIEWIFDDSKLYYGSDALRCVDEKFVIRKPFRGG
SFNVKSPYYKSLAELISDVTKLLEHALNSETLNVKPTKFNQYKVVLVIPDIFKKSHVETF
IRVLLTELQFQAVAIIQESLATCYGAGISTSTCVVNIGAAETRIACVDEGTVLEHSAITL
DYGGDDITRLFALFLLQSDFPLQDWKIDSKHGWLLAERLKKNFTTFQDADVAVQLYNFMN
RSPNQPTEKYEFKLFDEVMLAPLALFFPQIFKLIRTSSHKNSSLEFQLPESRDLFTNELN
DWNSLSQFESKEGNLYCDLNDDLKILNRILDAHNIIDQLQDKPENYGNTLKENFAPLEKA
IVQSIANASITADVTRMNSFYSNILIVGGSSKIPALDFILTDRINIWRPSLLSSASFPQF
YKKLTKEIKDLEGHYVNAPDKTEDENKQILQAQIKEKIVEELEEQHQNIEHQNGNEHIFP
VSIIPPPRDMNPALIIWKGASVLAQIKLVEELFITNSDWDVHGSRILQYKCIFTY

Primary citation

Interactions between the Nucleosome Histone Core and Arp8 in the Ino80 Chromatin Remodeling Complex. Saravanan, M., Wuerges, J., Bose, D. et al. Proc Natl Acad Sci U S A (2012) 109:20883. DOI 10.1073/PNAS.1214735109 · PubMed

Other PDB entries of the same protein (UniProt Q12386 (AlphaFold model), which also has an AlphaFold model), best resolution first:

8A5O 3.2 Å, Structure of Arp4-Ies4-N-actin-Arp8-Ino80HSA subcomplex (A-module) of S. cerevisiae INO80
4AM7 3.25 Å, ADP-bound C-terminal domain of actin-related protein ARP8 from S. Cerevisiae
8A5A 3.3 Å, Structure of Arp4-Ies4-N-actin-Arp8-Ino80HSA subcomplex (A-module) of INO80
5NBN 4.0 Å, Crystal structure of the Arp4-N-actin-Arp8-Ino80HSA module of INO80

Browse structure collections

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