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2M1R

PHD domain of ING4 N214D mutant

Functional Information from GO Data
ChainGOidnamespacecontents
A0005634cellular_componentnucleus
A0008285biological_processnegative regulation of cell population proliferation
A0016573biological_processhistone acetylation
A0070776cellular_componentMOZ/MORF histone acetyltransferase complex
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 301
ChainResidue
ACYS199
ACYS201
ATYR206
AHIS223
ACYS226

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 302
ChainResidue
ACYS242
ACYS212
ACYS217
APHE222
ACYS239

Functional Information from PROSITE/UniProt
site_idPS01359
Number of Residues44
DetailsZF_PHD_1 Zinc finger PHD-type signature. Cl.Chqvsygem.....................................IgCddpdCsiewFHfaCvglttkprgk...................................WfCprC
ChainResidueDetails
ACYS199-CYS242

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues49
DetailsZinc finger: {"description":"PHD-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00146","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"Q9UK53","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues4
DetailsSite: {"description":"Histone H3K4me3 binding","evidences":[{"source":"UniProtKB","id":"Q9UK53","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

243083

PDB entries from 2025-10-15

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