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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

6TU7

Structure of PfMyoA decorated Plasmodium Act1 filament

This is a non-PDB format compatible entry.
Functional Information from GO Data
ChainGOidnamespacecontents
AP10000146molecular_functionmicrofilament motor activity
AP10000166molecular_functionnucleotide binding
AP10003774molecular_functioncytoskeletal motor activity
AP10003779molecular_functionactin binding
AP10005515molecular_functionprotein binding
AP10005524molecular_functionATP binding
AP10005737cellular_componentcytoplasm
AP10005886cellular_componentplasma membrane
AP10007015biological_processactin filament organization
AP10015629cellular_componentactin cytoskeleton
AP10016020cellular_componentmembrane
AP10016459cellular_componentmyosin complex
AP10020039cellular_componentpellicle
AP10051015molecular_functionactin filament binding
AP10070258cellular_componentinner membrane pellicle complex
AP10160055cellular_componentglideosome
BP10000166molecular_functionnucleotide binding
BP10005200molecular_functionstructural constituent of cytoskeleton
BP10005515molecular_functionprotein binding
BP10005524molecular_functionATP binding
BP10005634cellular_componentnucleus
BP10005737cellular_componentcytoplasm
BP10005856cellular_componentcytoskeleton
BP10005884cellular_componentactin filament
BP10007010biological_processcytoskeleton organization
BP10009665biological_processplastid inheritance
BP10015629cellular_componentactin cytoskeleton
BP10016787molecular_functionhydrolase activity
BP10016887molecular_functionATP hydrolysis activity
BP10020014biological_processschizogony
BP10051701biological_processbiological process involved in interaction with host
BP10070360biological_processsymbiont-mediated actin polymerization-dependent cell-to-cell migration in host
BP10085017biological_processentry into host cell by a symbiont-containing vacuole
CP10000166molecular_functionnucleotide binding
CP10005200molecular_functionstructural constituent of cytoskeleton
CP10005515molecular_functionprotein binding
CP10005524molecular_functionATP binding
CP10005634cellular_componentnucleus
CP10005737cellular_componentcytoplasm
CP10005856cellular_componentcytoskeleton
CP10005884cellular_componentactin filament
CP10007010biological_processcytoskeleton organization
CP10009665biological_processplastid inheritance
CP10015629cellular_componentactin cytoskeleton
CP10016787molecular_functionhydrolase activity
CP10016887molecular_functionATP hydrolysis activity
CP10020014biological_processschizogony
CP10051701biological_processbiological process involved in interaction with host
CP10070360biological_processsymbiont-mediated actin polymerization-dependent cell-to-cell migration in host
CP10085017biological_processentry into host cell by a symbiont-containing vacuole
DP10000166molecular_functionnucleotide binding
DP10005200molecular_functionstructural constituent of cytoskeleton
DP10005515molecular_functionprotein binding
DP10005524molecular_functionATP binding
DP10005634cellular_componentnucleus
DP10005737cellular_componentcytoplasm
DP10005856cellular_componentcytoskeleton
DP10005884cellular_componentactin filament
DP10007010biological_processcytoskeleton organization
DP10009665biological_processplastid inheritance
DP10015629cellular_componentactin cytoskeleton
DP10016787molecular_functionhydrolase activity
DP10016887molecular_functionATP hydrolysis activity
DP10020014biological_processschizogony
DP10051701biological_processbiological process involved in interaction with host
DP10070360biological_processsymbiont-mediated actin polymerization-dependent cell-to-cell migration in host
DP10085017biological_processentry into host cell by a symbiont-containing vacuole
EP10000166molecular_functionnucleotide binding
EP10005200molecular_functionstructural constituent of cytoskeleton
EP10005515molecular_functionprotein binding
EP10005524molecular_functionATP binding
EP10005634cellular_componentnucleus
EP10005737cellular_componentcytoplasm
EP10005856cellular_componentcytoskeleton
EP10005884cellular_componentactin filament
EP10007010biological_processcytoskeleton organization
EP10009665biological_processplastid inheritance
EP10015629cellular_componentactin cytoskeleton
EP10016787molecular_functionhydrolase activity
EP10016887molecular_functionATP hydrolysis activity
EP10020014biological_processschizogony
EP10051701biological_processbiological process involved in interaction with host
EP10070360biological_processsymbiont-mediated actin polymerization-dependent cell-to-cell migration in host
EP10085017biological_processentry into host cell by a symbiont-containing vacuole
GP10000146molecular_functionmicrofilament motor activity
GP10000166molecular_functionnucleotide binding
GP10003774molecular_functioncytoskeletal motor activity
GP10003779molecular_functionactin binding
GP10005515molecular_functionprotein binding
GP10005524molecular_functionATP binding
GP10005737cellular_componentcytoplasm
GP10005886cellular_componentplasma membrane
GP10007015biological_processactin filament organization
GP10015629cellular_componentactin cytoskeleton
GP10016020cellular_componentmembrane
GP10016459cellular_componentmyosin complex
GP10020039cellular_componentpellicle
GP10051015molecular_functionactin filament binding
GP10070258cellular_componentinner membrane pellicle complex
GP10160055cellular_componentglideosome
Functional Information from PROSITE/UniProt
site_idPS00406
Number of Residues11
DetailsACTINS_1 Actins signature 1. FVGDEAQt.KRG
ChainResidueDetails
BP1PHE54-GLY64
site_idPS00432
Number of Residues9
DetailsACTINS_2 Actins signature 2. WITKeEYDE
ChainResidueDetails
BP1TRP357-GLU365
site_idPS01132
Number of Residues13
DetailsACTINS_ACT_LIKE Actins and actin-related proteins signature. LLTEApLNPkgNR
ChainResidueDetails
BP1LEU105-ARG117
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues20
DetailsRegion: {"description":"Actin-binding","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues14
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine; by PKG","evidences":[{"source":"PubMed","id":"26149123","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues84
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_FI5
Number of Residues20
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_FI6
Number of Residues4
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_FI7
Number of Residues4
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_FI8
Number of Residues4
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_FI9
Number of Residues4
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_FI10
Number of Residues4
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_FI11
Number of Residues4
DetailsSite: {"description":"Not methylated","evidences":[{"source":"PubMed","id":"31199804","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

239803

PDB entries from 2025-08-06

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