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2PNX

The PHD finger of ING4 in complex with an H3K4Me3 histone peptide

Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 300
ChainResidue
ACYS199
ACYS201
AHIS223
ACYS226

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 400
ChainResidue
ACYS212
ACYS217
ACYS239
ACYS242

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN C 300
ChainResidue
CCYS201
CHIS223
CCYS226
CCYS199

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN C 400
ChainResidue
CCYS212
CCYS217
CCYS239
CCYS242

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

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues98
DetailsZN_FING: PHD-type => ECO:0000255|PROSITE-ProRule:PRU00146
ChainResidueDetails
APRO196-GLU245
CPRO196-GLU245

site_idSWS_FT_FI2
Number of Residues16
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:Q9UK53
ChainResidueDetails
ACYS199
CCYS201
CCYS212
CCYS217
CHIS223
CCYS226
CCYS239
CCYS242
ACYS201
ACYS212
ACYS217
AHIS223
ACYS226
ACYS239
ACYS242
CCYS199

site_idSWS_FT_FI3
Number of Residues8
DetailsSITE: Histone H3K4me3 binding => ECO:0000250|UniProtKB:Q9UK53
ChainResidueDetails
ATYR198
AMET209
AASP213
ATRP221
CTYR198
CMET209
CASP213
CTRP221

218853

PDB entries from 2024-04-24

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