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3SOX

Structure of UHRF1 PHD finger in the free form

Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 1
ChainResidue
ACYS315
ACYS318
ACYS326
ACYS329

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 2
ChainResidue
ACYS331
ACYS334
AHIS354
ACYS357

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 3
ChainResidue
ACYS349
ACYS373
ACYS376
ACYS346

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 7
ChainResidue
AHIS332
AHIS332
AGLU375
AGLU375

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 4
ChainResidue
BCYS331
BCYS334
BHIS354
BCYS357

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 5
ChainResidue
BCYS315
BCYS318
BCYS326
BCYS329

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 6
ChainResidue
BCYS346
BCYS349
BCYS373
BCYS376

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 8
ChainResidue
BHIS332
BHIS332
BGLU375
BGLU375

Functional Information from PROSITE/UniProt
site_idPS01359
Number of Residues62
DetailsZF_PHD_1 Zinc finger PHD-type signature. CkhCkddvnrlcrvcachlcggrqdpdkq....................LmCde..Cdma.FHiyCldpplssvpsede................................WyCpeC
ChainResidueDetails
ACYS315-CYS376

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues12
DetailsRegion: {"description":"Histone H3R2me0 binding"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsSite: {"description":"Histone H3K4me0 binding"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues4
DetailsSite: {"description":"Histone H3R2me0 binding"}
ChainResidueDetails

239149

PDB entries from 2025-07-23

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