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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

7ALN

Cryo-EM structure of the divergent actomyosin complex from Plasmodium falciparum Myosin A in the Rigor state

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0005200molecular_functionstructural constituent of cytoskeleton
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005856cellular_componentcytoskeleton
A0005884cellular_componentactin filament
A0007010biological_processcytoskeleton organization
A0009665biological_processplastid inheritance
A0015629cellular_componentactin cytoskeleton
A0016787molecular_functionhydrolase activity
A0016887molecular_functionATP hydrolysis activity
A0020014biological_processschizogony
A0051701biological_processbiological process involved in interaction with host
A0070360biological_processsymbiont-mediated actin polymerization-dependent cell-to-cell migration in host
A0085017biological_processentry into host cell by a symbiont-containing vacuole
B0000166molecular_functionnucleotide binding
B0005200molecular_functionstructural constituent of cytoskeleton
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0005856cellular_componentcytoskeleton
B0005884cellular_componentactin filament
B0007010biological_processcytoskeleton organization
B0009665biological_processplastid inheritance
B0015629cellular_componentactin cytoskeleton
B0016787molecular_functionhydrolase activity
B0016887molecular_functionATP hydrolysis activity
B0020014biological_processschizogony
B0051701biological_processbiological process involved in interaction with host
B0070360biological_processsymbiont-mediated actin polymerization-dependent cell-to-cell migration in host
B0085017biological_processentry into host cell by a symbiont-containing vacuole
C0000166molecular_functionnucleotide binding
C0005200molecular_functionstructural constituent of cytoskeleton
C0005515molecular_functionprotein binding
C0005524molecular_functionATP binding
C0005634cellular_componentnucleus
C0005737cellular_componentcytoplasm
C0005856cellular_componentcytoskeleton
C0005884cellular_componentactin filament
C0007010biological_processcytoskeleton organization
C0009665biological_processplastid inheritance
C0015629cellular_componentactin cytoskeleton
C0016787molecular_functionhydrolase activity
C0016887molecular_functionATP hydrolysis activity
C0020014biological_processschizogony
C0051701biological_processbiological process involved in interaction with host
C0070360biological_processsymbiont-mediated actin polymerization-dependent cell-to-cell migration in host
C0085017biological_processentry into host cell by a symbiont-containing vacuole
D0000166molecular_functionnucleotide binding
D0005200molecular_functionstructural constituent of cytoskeleton
D0005515molecular_functionprotein binding
D0005524molecular_functionATP binding
D0005634cellular_componentnucleus
D0005737cellular_componentcytoplasm
D0005856cellular_componentcytoskeleton
D0005884cellular_componentactin filament
D0007010biological_processcytoskeleton organization
D0009665biological_processplastid inheritance
D0015629cellular_componentactin cytoskeleton
D0016787molecular_functionhydrolase activity
D0016887molecular_functionATP hydrolysis activity
D0020014biological_processschizogony
D0051701biological_processbiological process involved in interaction with host
D0070360biological_processsymbiont-mediated actin polymerization-dependent cell-to-cell migration in host
D0085017biological_processentry into host cell by a symbiont-containing vacuole
E0000166molecular_functionnucleotide binding
E0005200molecular_functionstructural constituent of cytoskeleton
E0005515molecular_functionprotein binding
E0005524molecular_functionATP binding
E0005634cellular_componentnucleus
E0005737cellular_componentcytoplasm
E0005856cellular_componentcytoskeleton
E0005884cellular_componentactin filament
E0007010biological_processcytoskeleton organization
E0009665biological_processplastid inheritance
E0015629cellular_componentactin cytoskeleton
E0016787molecular_functionhydrolase activity
E0016887molecular_functionATP hydrolysis activity
E0020014biological_processschizogony
E0051701biological_processbiological process involved in interaction with host
E0070360biological_processsymbiont-mediated actin polymerization-dependent cell-to-cell migration in host
E0085017biological_processentry into host cell by a symbiont-containing vacuole
F0000146molecular_functionmicrofilament motor activity
F0000166molecular_functionnucleotide binding
F0003774molecular_functioncytoskeletal motor activity
F0003779molecular_functionactin binding
F0005515molecular_functionprotein binding
F0005524molecular_functionATP binding
F0005737cellular_componentcytoplasm
F0005886cellular_componentplasma membrane
F0007015biological_processactin filament organization
F0015629cellular_componentactin cytoskeleton
F0016020cellular_componentmembrane
F0016459cellular_componentmyosin complex
F0020039cellular_componentpellicle
F0051015molecular_functionactin filament binding
F0070258cellular_componentinner membrane pellicle complex
F0160055cellular_componentglideosome
Functional Information from PROSITE/UniProt
site_idPS00406
Number of Residues11
DetailsACTINS_1 Actins signature 1. FVGDEAQt.KRG
ChainResidueDetails
APHE54-GLY64
site_idPS00432
Number of Residues9
DetailsACTINS_2 Actins signature 2. WITKeEYDE
ChainResidueDetails
ATRP357-GLU365
site_idPS01132
Number of Residues13
DetailsACTINS_ACT_LIKE Actins and actin-related proteins signature. LLTEApLNPkgNR
ChainResidueDetails
ALEU105-ARG117
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues105
DetailsRegion: {"description":"DNAseI-binding D loop; regulates polymerization and stability of the actin filament","evidences":[{"source":"UniProtKB","id":"Q4Z1L3","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues25
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"24743229","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"28695858","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"31199804","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"33767187","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JAN-2020","submissionDatabase":"PDB data bank","title":"Malaria parasite actomyosin rigor-state structure at near-atomic resolution.","authors":["Vahokoski J.","Calder L.J.","Lopez A.J.","Molloy J.E.","Rosenthal P.B.","Kursula I."]}},{"source":"PDB","id":"4CBU","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5MVV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6I4D","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6I4E","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6TU4","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7ALN","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues5
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"24743229","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"28695858","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"28923924","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"31199804","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JAN-2020","submissionDatabase":"PDB data bank","title":"Malaria parasite actomyosin rigor-state structure at near-atomic resolution.","authors":["Vahokoski J.","Calder L.J.","Lopez A.J.","Molloy J.E.","Rosenthal P.B.","Kursula I."]}},{"source":"PDB","id":"4CBU","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5MVV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5OGW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6I4D","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6I4E","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6TU4","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues5
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"24743229","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"28695858","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"28923924","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"31199804","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"33767187","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JAN-2020","submissionDatabase":"PDB data bank","title":"Malaria parasite actomyosin rigor-state structure at near-atomic resolution.","authors":["Vahokoski J.","Calder L.J.","Lopez A.J.","Molloy J.E.","Rosenthal P.B.","Kursula I."]}},{"source":"PDB","id":"4CBU","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5MVV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5OGW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6I4D","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6I4E","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6TU4","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7ALN","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues5
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"24743229","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"28695858","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"31199804","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4CBU","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5MVV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6I4D","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues5
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"24743229","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"28695858","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"28923924","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"31199804","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4CBU","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5MVV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5OGW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6I4D","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues5
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"24743229","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"28695858","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"31199804","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4CBU","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5MVV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6I4D","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6I4E","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues5
DetailsSite: {"description":"Not methylated","evidences":[{"source":"PubMed","id":"31199804","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues10
DetailsRegion: {"description":"Actin-binding","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues7
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine; by PKG","evidences":[{"source":"PubMed","id":"26149123","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

246905

PDB entries from 2025-12-31

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