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5U7G

Crystal Structure of the Catalytic Core of CBP

Functional Information from GO Data
ChainGOidnamespacecontents
A0004402molecular_functionhistone acetyltransferase activity
A0006355biological_processregulation of DNA-templated transcription
A0008270molecular_functionzinc ion binding
B0004402molecular_functionhistone acetyltransferase activity
B0006355biological_processregulation of DNA-templated transcription
B0008270molecular_functionzinc ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue ZN A 1801
ChainResidue
ACYS1200
ACYS1201
AHIS1292
ACYS1295

site_idAC2
Number of Residues4
Detailsbinding site for residue ZN A 1802
ChainResidue
ACYS1284
ACYS1287
ACYS1309
ACYS1312

site_idAC3
Number of Residues4
Detailsbinding site for residue ZN A 1803
ChainResidue
ACYS1711
ACYS1730
ACYS1733
ACYS1708

site_idAC4
Number of Residues4
Detailsbinding site for residue ZN A 1804
ChainResidue
ACYS1721
ACYS1724
AHIS1739
AHIS1741

site_idAC5
Number of Residues4
Detailsbinding site for residue ZN B 1801
ChainResidue
BCYS1200
BCYS1201
BHIS1292
BCYS1295

site_idAC6
Number of Residues4
Detailsbinding site for residue ZN B 1802
ChainResidue
BCYS1284
BCYS1287
BCYS1309
BCYS1312

site_idAC7
Number of Residues4
Detailsbinding site for residue ZN B 1803
ChainResidue
BCYS1708
BCYS1711
BCYS1730
BCYS1733

site_idAC8
Number of Residues4
Detailsbinding site for residue ZN B 1804
ChainResidue
BCYS1721
BCYS1724
BHIS1739
BHIS1741

Functional Information from PROSITE/UniProt
site_idPS00633
Number of Residues60
DetailsBROMODOMAIN_1 Bromodomain signature. SlpFrqpvDpqllgipDYFdiVknpMdlstIkrkldtgq..Yqepwqyvddvwl.MfnNAwlY
ChainResidueDetails
ASER1109-TYR1168

site_idPS01357
Number of Residues26
DetailsZF_ZZ_1 Zinc finger ZZ-type signature. CneCkhhvet..RWhCtv...CeDYdLCinC
ChainResidueDetails
ACYS1708-CYS1733

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues214
DetailsDomain: {"description":"Bromo","evidences":[{"source":"PROSITE-ProRule","id":"PRU00035","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues96
DetailsZinc finger: {"description":"ZZ-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00228","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues92
DetailsRegion: {"description":"Interaction with histone","evidences":[{"source":"UniProtKB","id":"Q92793","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues36
DetailsRegion: {"description":"Interaction with ASF1A","evidences":[{"source":"UniProtKB","id":"Q92793","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues4
DetailsRegion: {"description":"Interaction with histone","evidences":[{"source":"UniProtKB","id":"Q09472","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues12
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"Q09472","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues16
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00228","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues4
DetailsModified residue: {"description":"Phosphoserine; by IKKA","evidences":[{"source":"UniProtKB","id":"Q92793","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q92793","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"23806337","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

247947

PDB entries from 2026-01-21

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