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5XFN

Structure of the N-terminal domains of PHF1

Functional Information from GO Data
ChainGOidnamespacecontents
A0006974biological_processcellular response to DNA damage stimulus
A0031060biological_processregulation of histone methylation
A0035064molecular_functionmethylated histone binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue ZN A 401
ChainResidue
ACYS107
ACYS110
ACYS136
ACYS139

site_idAC2
Number of Residues4
Detailsbinding site for residue ZN A 402
ChainResidue
ACYS90
ACYS93
AHIS115
ACYS118

site_idAC3
Number of Residues4
Detailsbinding site for residue ZN A 403
ChainResidue
ACYS191
AHIS212
ACYS215
ACYS189

site_idAC4
Number of Residues4
Detailsbinding site for residue ZN A 404
ChainResidue
ACYS204
ACYS207
ACYS234
ACYS237

Functional Information from PROSITE/UniProt
site_idPS01359
Number of Residues50
DetailsZF_PHD_1 Zinc finger PHD-type signature. CcvCrsetvvpgnrl..................................VsCek..Crha.YHqdChvprapapgegegts..............................WvCrqC
ChainResidueDetails
ACYS90-CYS139
ACYS189-CYS237

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues55
DetailsZN_FING: PHD-type 1 => ECO:0000255|PROSITE-ProRule:PRU00146
ChainResidueDetails
AGLU87-ALA142

site_idSWS_FT_FI2
Number of Residues54
DetailsZN_FING: PHD-type 2 => ECO:0000255|PROSITE-ProRule:PRU00146
ChainResidueDetails
AGLN186-GLY240

218853

PDB entries from 2024-04-24

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