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7KKF

Crystal Structure of S. cerevisiae Ess1

Functional Information from GO Data
ChainGOidnamespacecontents
A0000122biological_processnegative regulation of transcription by RNA polymerase II
A0000993molecular_functionRNA polymerase II complex binding
A0003755molecular_functionpeptidyl-prolyl cis-trans isomerase activity
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006369biological_processtermination of RNA polymerase II transcription
A0016853molecular_functionisomerase activity
A0045899biological_processpositive regulation of RNA polymerase II transcription preinitiation complex assembly
A0045944biological_processpositive regulation of transcription by RNA polymerase II
A0060261biological_processpositive regulation of transcription initiation by RNA polymerase II
A2000059biological_processnegative regulation of ubiquitin-dependent protein catabolic process
A2000749biological_processpositive regulation of rDNA heterochromatin formation
B0000122biological_processnegative regulation of transcription by RNA polymerase II
B0000993molecular_functionRNA polymerase II complex binding
B0003755molecular_functionpeptidyl-prolyl cis-trans isomerase activity
B0005515molecular_functionprotein binding
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006369biological_processtermination of RNA polymerase II transcription
B0016853molecular_functionisomerase activity
B0045899biological_processpositive regulation of RNA polymerase II transcription preinitiation complex assembly
B0045944biological_processpositive regulation of transcription by RNA polymerase II
B0060261biological_processpositive regulation of transcription initiation by RNA polymerase II
B2000059biological_processnegative regulation of ubiquitin-dependent protein catabolic process
B2000749biological_processpositive regulation of rDNA heterochromatin formation
Functional Information from PROSITE/UniProt
site_idPS01096
Number of Residues21
DetailsPPIC_PPIASE_1 PpiC-type peptidyl-prolyl cis-trans isomerase signature. FEaLAkerSdcs.Sykr..GGdLG
ChainResidueDetails
APHE110-GLY130

site_idPS01159
Number of Residues27
DetailsWW_DOMAIN_1 WW/rsp5/WWP domain signature. WtvryskskkreYFfnpetkhSQWEEP
ChainResidueDetails
ATRP15-PRO41

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues34
DetailsDomain: {"description":"WW","evidences":[{"source":"PROSITE-ProRule","id":"PRU00224","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues226
DetailsDomain: {"description":"PpiC","evidences":[{"source":"PROSITE-ProRule","id":"PRU00278","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues23
DetailsRegion: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues21
DetailsCompositional bias: {"description":"Basic and acidic residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18407956","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

245663

PDB entries from 2025-12-03

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