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3IO2

Crystal structure of the Taz2 domain of p300

Functional Information from GO Data
ChainGOidnamespacecontents
A0004402molecular_functionhistone acetyltransferase activity
A0006355biological_processregulation of DNA-templated transcription
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 201
ChainResidue
AHIS1744
ACYS1748
ACYS1753
ACYS1758

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 202
ChainResidue
AHIS1767
ACYS1771
ACYS1779
ACYS1782

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 203
ChainResidue
ACYS1796
ACYS1801
ACYS1806
AHIS1792

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 204
ChainResidue
ACYS1771
ALYS1772
AARG1773

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 205
ChainResidue
AHOH30
AARG1737
AARG1737
AGLN1740
APRO1756
ASER1757

site_idAC6
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 A 206
ChainResidue
AGLN1784
AARG1829

site_idAC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 207
ChainResidue
AARG1773
AGLN1811
AARG1814

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues81
DetailsZN_FING: TAZ-type 2 => ECO:0000255|PROSITE-ProRule:PRU00203
ChainResidueDetails
AGLY1728-ILE1809

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER1726

237423

PDB entries from 2025-06-11

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