6YW7: ARP2/3 1A5C isoform complex

Cryo-EM structure of the ARP2/3 1A5C isoform complex. Determined by electron microscopy at 4.5 Å resolution. Released 22 Jul 2020.

Method
Electron microscopy
Resolution
4.5 Å
Organism
Homo sapiens
Chains
7
Atoms
5,426
Mol. weight
225.88 kDa
Ligands
ATP
Released
22 Jul 2020

Explore 6YW7 in 3D Show helices and sheets RCSB PDB PDBe

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Actin-related protein 3Aprotein418Homo sapiensP61158 (AlphaFold model)
Actin-related protein 2/3 complex subunit 2Dprotein300Homo sapiensO15144 (AlphaFold model)
Actin-related protein 2/3 complex subunit 3Eprotein178Homo sapiensO15145 (AlphaFold model)
Actin-related protein 2Bprotein394Homo sapiensP61160 (AlphaFold model)
Actin-related protein 2/3 complex subunit 4Fprotein168Homo sapiensP59998
Actin-related protein 2/3 complex subunit 5Gprotein151Homo sapiensO15511
Actin-related protein 2/3 complex subunit 1ACprotein370Homo sapiensQ92747
Sequence of entity 1 (A), FASTA
>6YW7_1 Actin-related protein 3 (chains A)
MAGRLPACVVDCGTGYTKLGYAGNTEPQFIIPSCIAIKESAKVGDQAQRRVMKGVDDLDF
FIGDEAIEKPTYATKWPIRHGIVEDWDLMERFMEQVIFKYLRAEPEDHYFLLTEPPLNTP
ENREYTAEIMFESFNVPGLYIAVQAVLALAASWTSRQVGERTLTGTVIDSGDGVTHVIPV
AEGYVIGSCIKHIPIAGRDITYFIQQLLRDREVGIPPEQSLETAKAVKERYSYVCPDLVK
EFNKYDTDGSKWIKQYTGINAISKKEFSIDVGYERFLGPEIFFHPEFANPDFTQPISEVV
DEVIQNCPIDVRRPLYKNIVLSGGSTMFRDFGRRLQRDLKRTVDARLKLSEELSGGRLKP
KPIDVQVITHHMQRYAVWFGGSMLASTPEFYQVCHTKKDYEEIGPSICRHNPVFGVMS
Sequence of entity 2 (D), FASTA
>6YW7_2 Actin-related protein 2/3 complex subunit 2 (chains D)
MILLEVNNRIIEETLALKFENAAAGNKPEAVEVTFADFDGVLYHISNPNGDKTKVMVSIS
LKFYKELQAHGADELLKRVYGSFLVNPESGYNVSLLYDLENLPASKDSIVHQAGMLKRNC
FASVFEKYFQFQEEGKEGENRAVIHYRDDETMYVESKKDRVTVVFSTVFKDDDDVVIGKV
FMQEFKEGRRASHTAPQVLFSHREPPLELKDTDAAVGDNIGYITFVLFPRHTNASARDNT
INLIHTFRDYLHYHIKCSKAYIHTRMRAKTSDFLKVLNRARPDAEKKEMKTITGKTFSSR
Sequence of entity 3 (E), FASTA
>6YW7_3 Actin-related protein 2/3 complex subunit 3 (chains E)
MPAYHSSLMDPDTKLIGNMALLPIRSQFKGPAPRETKDTDIVDEAIYYFKANVFFKNYEI
KNEADRTLIYITLYISECLKKLQKCNSKSQGEKEMYTLGITNFPIPGEPGFPLNAIYAKP
ANKQEDEVMRAYLQQLRQETGLRLCEKVFDPQNDKPSKWWTCFVKRQFMNKSLSGPGQ
Sequence of entity 4 (B), FASTA
>6YW7_4 Actin-related protein 2 (chains B)
MDSQGRKVVVCDNGTGFVKCGYAGSNFPEHIFPAIVGRPIIRSTTKVGNIEIKDLMVGDE
ASELRSMLEVNYPMENGIVRNWDDMKHLWDYTFGPEKLNIDTRNCKILLTEPPMNPTKNR
EKIVEVMFETYQFSGVYVAIQAVLTLYAQGLLTGVVVDSGDGVTHICPVYEGFSLPHLTR
RLDIAGRDITRYLIKLLLLRGYAFNHSADFETVRMIKEKLCYVGYNIEQEQKLALETTVL
VESYTLPDGRIIKVGGERFEAPEALFQPHLINVEGVGVAELLFNTIQAADIDTRSEFYKH
IVLSGGSTMYPGLPSRLERELKQLYLERVLKGDVEKLSKFKIRIEDPPRRKHMVFLGGAV
LADIMKDKDNFWMTRQEYQEKGVRVLEKLGVTVR
Sequence of entity 5 (F), FASTA
>6YW7_5 Actin-related protein 2/3 complex subunit 4 (chains F)
MTATLRPYLSAVRATLQAALCLENFSSQVVERHNKPEVEVRSSKELLLQPVTISRNEKEK
VLIEGSINSVRVSIAVKQADEIEKILCHKFMRFMMMRAENFFILRRKPVEGYDISFLITN
FHTEQMYKHKLVDFVIHFMEEIDKEISEMKLSVNARARIVAEEFLKNF
Sequence of entity 6 (G), FASTA
>6YW7_6 Actin-related protein 2/3 complex subunit 5 (chains G)
MSKNTVSSARFRKVDVDEYDENKFVDEEDGGDGQAGPDEGEVDSCLRQGNMTAALQAALK
NPPINTKSQAVKDRAGSIVLKVLISFKANDIEKAVQSLDKNGVDLLMKYIYKGFESPSDN
SSAMLLQWHEKALAAGGVGSIVRVLTARKTV
Sequence of entity 7 (C), FASTA
>6YW7_7 Actin-related protein 2/3 complex subunit 1A (chains C)
MSLHQFLLEPITCHAWNRDRTQIALSPNNHEVHIYKKNGSQWVKAHELKEHNGHITGIDW
APKSDRIVTCGADRNAYVWSQKDGVWKPTLVILRINRAATFVKWSPLENKFAVGSGARLI
SVCYFESENDWWVSKHIKKPIRSTVLSLDWHPNNVLLAAGSCDFKCRVFSAYIKEVDEKP
ASTPWGSKMPFGQLMSEFGGSGTGGWVHGVSFSASGSRLAWVSHDSTVSVADASKSVQVS
TLKTEFLPLLSVSFVSENSVVAAGHDCCPMLFNYDDRGCLTFVSKLDIPKQSIQRNMSAM
ERFRNMDKRATTEDRNTALETLHQNSITQVSIYEVDKQDCRKFCTTGIDGAMTIWDFKTL
ESSIQGLRIM

Ligands and cofactors

IDNameFormulaCopies
ATPAdenosine-5'-triphosphateC10 H16 N5 O13 P32

Primary citation

Cryo-EM of human Arp2/3 complexes provides structural insights into actin nucleation modulation by ARPC5 isoforms. von Loeffelholz, O., Purkiss, A., Cao, L. et al. Biol Open (2020) 9. DOI 10.1242/bio.054304 · PubMed

Other PDB entries of the same protein (UniProt P61158 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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