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1P4Q

Solution structure of the CITED2 transactivation domain in complex with the p300 CH1 domain

Functional Information from GO Data
ChainGOidnamespacecontents
A0005634cellular_componentnucleus
A0006355biological_processregulation of DNA-templated transcription
B0004402molecular_functionhistone acetyltransferase activity
B0006355biological_processregulation of DNA-templated transcription
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 301
ChainResidue
BHIS125
BCYS129
BCYS142
BCYS147

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 302
ChainResidue
BHIS156
BCYS160
BCYS166
BCYS171

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN B 303
ChainResidue
BCYS184
BCYS189
BVAL191
BCYS192
BHIS180

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues86
DetailsZN_FING: TAZ-type 1 => ECO:0000255|PROSITE-ProRule:PRU00203
ChainResidueDetails
BASP109-LEU195

site_idSWS_FT_FI2
Number of Residues12
DetailsBINDING: BINDING => ECO:0000269|PubMed:11959990, ECO:0000269|PubMed:12778114
ChainResidueDetails
BHIS125
BCYS184
BCYS189
BCYS192
BCYS129
BCYS142
BCYS147
BHIS156
BCYS160
BCYS166
BCYS171
BHIS180

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0000269|PubMed:18995842
ChainResidueDetails
BLYS196
BLYS201

225946

PDB entries from 2024-10-09

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