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6ZZ6

Cryo-EM structure of S.cerevisiae cohesin-Scc2-DNA complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0005524molecular_functionATP binding
A0007062biological_processsister chromatid cohesion
A0008278cellular_componentcohesin complex
A0016887molecular_functionATP hydrolysis activity
B0005524molecular_functionATP binding
B0016887molecular_functionATP hydrolysis activity
C0007062biological_processsister chromatid cohesion
C0008278cellular_componentcohesin complex
D0000775cellular_componentchromosome, centromeric region
D0000785cellular_componentchromatin
D0000972biological_processtranscription-dependent tethering of RNA polymerase II gene DNA at nuclear periphery
D0003682molecular_functionchromatin binding
D0005515molecular_functionprotein binding
D0005634cellular_componentnucleus
D0005729cellular_component2-micrometer circle DNA
D0005829cellular_componentcytosol
D0006302biological_processdouble-strand break repair
D0006351biological_processDNA-templated transcription
D0007064biological_processmitotic sister chromatid cohesion
D0007076biological_processmitotic chromosome condensation
D0010468biological_processregulation of gene expression
D0032116cellular_componentSMC loading complex
D0034087biological_processestablishment of mitotic sister chromatid cohesion
D0043515molecular_functionkinetochore binding
D0043565molecular_functionsequence-specific DNA binding
D0061775molecular_functioncohesin loader activity
D0070058biological_processtRNA gene clustering
D0070550biological_processrDNA chromatin condensation
D0071168biological_processprotein localization to chromatin
D0071169biological_processestablishment of protein localization to chromatin
D0090694cellular_componentScc2-Scc4 cohesin loading complex
D0140588biological_processchromatin looping
D1990414biological_processreplication-born double-strand break repair via sister chromatid exchange
Functional Information from PROSITE/UniProt
site_idPS00211
Number of Residues15
DetailsABC_TRANSPORTER_1 ABC transporters family signature. LSGGEKTVAALALLF
ChainResidueDetails
ALEU1129-PHE1143

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsMotif: {"description":"Nuclear localization signal","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues7
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"18614053","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues37
DetailsRepeat: {"description":"HEAT 1"}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues37
DetailsRepeat: {"description":"HEAT 2"}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues37
DetailsRepeat: {"description":"HEAT 3"}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues37
DetailsRepeat: {"description":"HEAT 4"}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues37
DetailsRepeat: {"description":"HEAT 5"}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues2
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"26354421","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues4
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"26354421","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine; in mutant scc2-8A","evidences":[{"source":"PubMed","id":"26354421","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine; in mutant scc2-8A","evidences":[{"source":"PubMed","id":"26354421","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

247536

PDB entries from 2026-01-14

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