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3SHB

Crystal Structure of PHD Domain of UHRF1

Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 1001
ChainResidue
ACYS315
ACYS318
ACYS326
ACYS329

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 1002
ChainResidue
ACYS331
ACYS334
AHIS354
ACYS357

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 1003
ChainResidue
ACYS349
ACYS373
ACYS376
ACYS346

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 1004
ChainResidue
AHIS332
AHIS332
AGLU375
AGLU375

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 Residues6
DetailsRegion: {"description":"Histone H3R2me0 binding"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsSite: {"description":"Histone H3K4me0 binding"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsSite: {"description":"Histone H3R2me0 binding"}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine; by PKA","evidences":[{"source":"PubMed","id":"15178447","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22837395","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

243911

PDB entries from 2025-10-29

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