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2R10

Structure of an acetylated Rsc4 tandem bromodomain Histone Chimera

Functional Information from GO Data
ChainGOidnamespacecontents
A0006338biological_processchromatin remodeling
A0016586cellular_componentRSC-type complex
B0006338biological_processchromatin remodeling
B0016586cellular_componentRSC-type complex
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 788
ChainResidue
ALYS174
AHIS177
AGLU296
AHOH989

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 789
ChainResidue
APRO56
ALYS57
APHE61
APHE64

Functional Information from PROSITE/UniProt
site_idPS00633
Number of Residues57
DetailsBROMODOMAIN_1 Bromodomain signature. FkdFiklpSrkfhp..QYYykIqqpMsineIksrdye....YedgpsnflldvelLtkNCqaY
ChainResidueDetails
APHE77-TYR133
ASER210-PHE267

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues210
DetailsDomain: {"description":"Bromo 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00035","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues222
DetailsDomain: {"description":"Bromo 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00035","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"19779198","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

250059

PDB entries from 2026-03-04

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