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2LN0

Structure of MOZ

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 Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 401
ChainResidue
ACYS209
ACYS212
AASN219
AHIS238
ACYS241

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 501
ChainResidue
ACYS230
ACYS233
ACYS259
ACYS262

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 601
ChainResidue
ACYS281
ACYS284
ACYS307
ACYS310

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 701
ChainResidue
ACYS265
ACYS268
AHIS289
ACYS292

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
DetailsZN_FING: PHD-type 1 => ECO:0000255|PROSITE-ProRule:PRU00146
ChainResidueDetails
AILE206-CYS265

site_idSWS_FT_FI2
Number of Residues54
DetailsZN_FING: PHD-type 2 => ECO:0000255|PROSITE-ProRule:PRU00146
ChainResidueDetails
ACYS259-ARG313

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PDB entries from 2024-07-24

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