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4LJN

Crystal Structure of MOZ double PHD finger

Functional Information from GO Data
ChainGOidnamespacecontents
A0003713molecular_functiontranscription coactivator activity
A0004402molecular_functionhistone acetyltransferase activity
A0005634cellular_componentnucleus
A0043966biological_processhistone H3 acetylation
A0048513biological_processanimal organ development
A0070776cellular_componentMOZ/MORF histone acetyltransferase complex
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 401
ChainResidue
ACYS281
ACYS284
ACYS307
ACYS310

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 402
ChainResidue
ACYS265
ACYS268
AHIS289
ACYS292

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 403
ChainResidue
ACYS212
AHIS238
ACYS241
ACYS209

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 404
ChainResidue
ACYS230
ACYS233
ACYS259
ACYS262

Functional Information from PROSITE/UniProt
site_idPS01359
Number of Residues81
DetailsZF_PHD_1 Zinc finger PHD-type signature. CadCgnsghpsclkfspeltvrvkalrwqciecktcsscrdqgknadnmLfCds..Cdrg.FHmeCcdppltrmpkgm.................................WiCqiC
ChainResidueDetails
ACYS230-CYS310

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues59
DetailsZinc finger: {"description":"PHD-type 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00146","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

239492

PDB entries from 2025-07-30

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