Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

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 Residues10
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:Q09472
ChainResidueDetails
ALEU1435
BTRP1503
AARG1447
AILE1494
AARG1499
ATRP1503
BLEU1435
BARG1447
BILE1494
BARG1499

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:23806337
ChainResidueDetails
ALYS1217
BLYS1217

site_idSWS_FT_FI3
Number of Residues4
DetailsMOD_RES: Phosphoserine; by IKKA => ECO:0000250|UniProtKB:Q92793
ChainResidueDetails
ASER1383
ASER1387
BSER1383
BSER1387

224201

PDB entries from 2024-08-28

PDB statisticsPDBj update infoContact PDBjnumon