4AM7: Actin-like protein ARP8

ADP-bound C-terminal domain of actin-related protein ARP8 from S. Cerevisiae. Determined by X-ray diffraction at 3.25 Å resolution. Released 12 Dec 2012.

Method
X-ray diffraction
Resolution
3.25 Å
Organism
SACCHAROMYCES CEREVISIAE
Chains
2
Atoms
10,126
Mol. weight
150.48 kDa
Ligands
ADP
Released
12 Dec 2012

Explore 4AM7 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4AM7 contains 73 α-helices and 56 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: 37 helices, 27 β-strands

ElementResiduesLengthSheet
α-helix265-2673
β-strand268-27251
β-strand277-28151
β-strand289-29241
β-strand295-29842
α-helix299-3013
α-helix321-34121
α-helix352-3543
β-strand358-35923
α-helix360-3612
β-strand37714
β-strand384-38522
α-helix387-3904
β-strand39214
β-strand397-40042
β-strand403-40425
β-strand407-40825
α-helix418-43316
β-strand43416
β-strand43916
α-helix442-4476
β-strand449-45461
α-helix460-47213
β-strand478-48361
α-helix484-4907
β-strand498-50367
β-strand508-51477
β-strand517-526107
α-helix530-54314
α-helix556-56914
α-helix574-5763
β-strand580-58673
β-strand594-60073
α-helix603-6097
α-helix610-6123
α-helix615-6195
α-helix622-6243
α-helix628-6314
α-helix635-6373
β-strand63818
β-strand64518
α-helix651-6577
α-helix662-6643
α-helix668-6758
α-helix678-6869
α-helix703-71614
α-helix720-7223
α-helix723-7275
β-strand730-73347
α-helix735-7384
α-helix742-75312
α-helix756-7583
β-strand76019
α-helix763-77816
α-helix798-81417
β-strand82419
β-strand829-83027
α-helix831-8333
α-helix838-8403
α-helix841-8499
α-helix854-8585
β-strand860-86121
α-helix862-8687
α-helix869-8746
Chain B: 36 helices, 29 β-strands
ElementResiduesLengthSheet
α-helix265-2673
β-strand268-273610
β-strand277-281510
α-helix2881
β-strand289-292410
β-strand295-298411
α-helix299-3013
β-strand315112
α-helix321-34121
β-strand377113
β-strand384-385211
α-helix387-3904
β-strand392113
β-strand397-400411
β-strand403114
β-strand408114
α-helix418-43215
α-helix442-4476
β-strand449-454610
α-helix460-4689
α-helix469-4735
β-strand478-479215
β-strand480-483410
α-helix484-4918
β-strand498-503616
β-strand508-513616
β-strand518116
α-helix520-5223
β-strand524-526316
α-helix530-54213
β-strand552112
α-helix556-56914
β-strand580-584517
β-strand596-600517
α-helix603-6097
α-helix610-6123
α-helix615-6206
α-helix622-6243
α-helix628-6336
α-helix635-6373
β-strand638118
β-strand645118
α-helix651-6588
α-helix668-6769
α-helix678-6858
α-helix703-71715
α-helix720-7223
α-helix723-7275
β-strand730-731219
β-strand732-733216
α-helix742-75312
α-helix756-7594
β-strand760120
α-helix763-77210
α-helix776-7794
α-helix797-81317
β-strand824120
β-strand829-830219
α-helix831-8322
α-helix841-8499
α-helix855-8573
β-strand860-861215
α-helix862-8687
α-helix869-8713
α-helix872-8754

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Actin-like protein ARP8A, Bprotein655SACCHAROMYCES CEREVISIAEQ12386 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>4AM7_1 ACTIN-LIKE PROTEIN ARP8 (chains A, B)
MGSSHHHHHHSSGLVPRGSHMHSEASAAPLNDEIDLNDPTATIVIHPGSNSIKIGFPKDD
HPVVVPNCVAVPKKWLDLENSEHVENVCLQREQSEEFNNIKSEMEKNFRERMRYYKRKVP
GNAHEQVVSFNENSKPEIISEKNDPSPIEWIFDDSKLYYGSDALRCVDEKFVIRKPFRGG
SFNVKSPYYKSLAELISDVTKLLEHALNSETLNVKPTKFNQYKVVLVIPDIFKKSHVETF
IRVLLTELQFQAVAIIQESLATCYGAGISTSTCVVNIGAAETRIACVDEGTVLEHSAITL
DYGGDDITRLFALFLLQSDFPLQDWKIDSKHGWLLAERLKKNFTTFQDADVAVQLYNFMN
RSPNQPTEKYEFKLFDEVMLAPLALFFPQIFKLIRTSSHKNSSLEFQLPESRDLFTNELN
DWNSLSQFESKEGNLYCDLNDDLKILNRILDAHNIIDQLQDKPENYGNTLKENFAPLEKA
IVQSIANASITADVTRMNSFYSNILIVGGSSKIPALDFILTDRINIWRPSLLSSASFPQF
YKKLTKEIKDLEGHYVNAPDKTEDENKQILQAQIKEKIVEELEEQHQNIEHQNGNEHIFP
VSIIPPPRDMNPALIIWKGASVLAQIKLVEELFITNSDWDVHGSRILQYKCIFTY

Ligands and cofactors

IDNameFormulaCopies
ADPAdenosine-5'-diphosphateC10 H15 N5 O10 P22

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:

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