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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
D0005694cellular_componentchromosome
D0005729cellular_component2-micrometer circle DNA
D0005829cellular_componentcytosol
D0006302biological_processdouble-strand break repair
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
D0061780biological_processmitotic cohesin loading
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
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 Residues5
DetailsMOD_RES: Phosphoserine; in mutant scc2-8A => ECO:0000269|PubMed:26354421
ChainResidueDetails
DSER43
DSER74
DSER162
DSER1179
DSER1183

site_idSWS_FT_FI2
Number of Residues3
DetailsMOD_RES: Phosphothreonine => ECO:0000269|PubMed:26354421
ChainResidueDetails
DTHR67
DTHR231
DTHR236

site_idSWS_FT_FI3
Number of Residues8
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:26354421
ChainResidueDetails
DSER127
DSER157
DSER163
DSER305
DSER320
DSER753
DSER1182
DSER1185

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphothreonine; in mutant scc2-8A => ECO:0000269|PubMed:26354421
ChainResidueDetails
DTHR360

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:18407956
ChainResidueDetails

223166

PDB entries from 2024-07-31

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