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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

5OGW

Cryo-EM structure of jasplakinolide-stabilized malaria parasite F-actin at near-atomic resolution

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
Functional Information from PDB Data
site_idAC1
Number of Residues14
Detailsbinding site for residue ADP A 401
ChainResidue
AGLY16
AGLU217
AGLY305
ATHR306
ATYR309
AMG402
ASER17
AASN19
ALYS21
AGLY159
AASP160
AGLY185
AARG213
ALYS216
site_idAC2
Number of Residues2
Detailsbinding site for residue MG A 402
ChainResidue
AGLN140
AADP401
site_idAC3
Number of Residues15
Detailsbinding site for residue 9UE A 403
ChainResidue
AHIS197
AGLY200
ATYR201
AGLY202
APHE203
AGLU208
ALEU245
AASN249
BVAL290
DHIS76
DILE78
DPRO115
DGLY117
DARG180
DASP182
site_idAC4
Number of Residues13
Detailsbinding site for residue ADP B 401
ChainResidue
BGLY16
BSER17
BASN19
BLYS21
BGLY159
BASP160
BARG213
BLYS216
BGLU217
BGLY305
BTHR306
BTYR309
BMG402
site_idAC5
Number of Residues2
Detailsbinding site for residue MG B 402
ChainResidue
BGLN140
BADP401
site_idAC6
Number of Residues13
Detailsbinding site for residue ADP C 401
ChainResidue
CGLY16
CSER17
CASN19
CLYS21
CGLY159
CASP160
CARG213
CLYS216
CGLU217
CGLY305
CTHR306
CTYR309
CMG402
site_idAC7
Number of Residues2
Detailsbinding site for residue MG C 402
ChainResidue
CGLN140
CADP401
site_idAC8
Number of Residues15
Detailsbinding site for residue 9UE C 403
ChainResidue
AVAL290
CHIS197
CGLY200
CTYR201
CGLY202
CPHE203
CGLU208
CLEU245
CASN249
CILE251
EHIS76
EILE78
EPRO115
EGLY117
EARG180
site_idAC9
Number of Residues13
Detailsbinding site for residue ADP D 401
ChainResidue
DGLY16
DSER17
DASN19
DLYS21
DGLY159
DASP160
DARG213
DLYS216
DGLU217
DGLY305
DTHR306
DTYR309
DMG402
site_idAD1
Number of Residues2
Detailsbinding site for residue MG D 402
ChainResidue
DGLN140
DADP401
site_idAD2
Number of Residues13
Detailsbinding site for residue ADP E 401
ChainResidue
EGLU217
EGLY305
ETHR306
ETYR309
EMG402
EGLY16
ESER17
EASN19
ELYS21
EGLY159
EASP160
EARG213
ELYS216
site_idAD3
Number of Residues2
Detailsbinding site for residue MG E 402
ChainResidue
EGLN140
EADP401
site_idAD4
Number of Residues14
Detailsbinding site for residue 9UE E 403
ChainResidue
AHIS76
AILE78
APRO115
AARG180
AASP182
DVAL290
EHIS197
EGLY200
ETYR201
EGLY202
EPHE203
EGLU208
ELEU245
EASN249
Functional Information from PROSITE/UniProt
site_idPS00406
Number of Residues11
DetailsACTINS_1 Actins signature 1. FVGDEAQt.KRG
ChainResidueDetails
APHE56-GLY66
site_idPS00432
Number of Residues9
DetailsACTINS_2 Actins signature 2. WITKeEYDE
ChainResidueDetails
ATRP359-GLU367
site_idPS01132
Number of Residues13
DetailsACTINS_ACT_LIKE Actins and actin-related proteins signature. LLTEApLNPkgNR
ChainResidueDetails
ALEU107-ARG119
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

246704

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