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8XV4

Crystal structure of TTD-PHD domain of UHRF1 in complex with mStella peptide (residues 85-119)

Functional Information from PROSITE/UniProt
site_idPS01359
Number of Residues62
DetailsZF_PHD_1 Zinc finger PHD-type signature. CkhCkddvnrlcrvcachlcggrqdpdkq....................LmCde..Cdma.FHiyCldpplssvpsede................................WyCpeC
ChainResidueDetails
ACYS302-CYS363

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues112
DetailsZN_FING: PHD-type => ECO:0000255|PROSITE-ProRule:PRU00146
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsSITE: Histone H3K4me0 binding
ChainResidueDetails
AGLN325
BGLN325

site_idSWS_FT_FI3
Number of Residues4
DetailsSITE: Histone H3R2me0 binding
ChainResidueDetails
ACYS336
AALA339
BCYS336
BALA339

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q8VDF2
ChainResidueDetails
ASER165
BSER165

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18220336, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163
ChainResidueDetails
AARG296
BARG296

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: Phosphoserine; by PKA => ECO:0000269|PubMed:15178447, ECO:0000269|PubMed:22837395
ChainResidueDetails
AASP307
BASP307

site_idSWS_FT_FI7
Number of Residues4
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733
ChainResidueDetails
APRO288
BPRO288

237735

PDB entries from 2025-06-18

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