Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

5XFP

Binary complex of PHF1 and a double stranded DNA

Functional Information from GO Data
ChainGOidnamespacecontents
A0006974biological_processcellular response to DNA damage stimulus
A0031060biological_processregulation of histone methylation
A0035064molecular_functionmethylated histone binding
B0006974biological_processcellular response to DNA damage stimulus
B0031060biological_processregulation of histone methylation
B0035064molecular_functionmethylated histone binding
E0006974biological_processcellular response to DNA damage stimulus
E0031060biological_processregulation of histone methylation
E0035064molecular_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
ACYS189
ACYS191
AHIS212
ACYS215

site_idAC3
Number of Residues4
Detailsbinding site for residue ZN A 403
ChainResidue
ACYS93
AHIS115
ACYS118
ACYS90

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

site_idAC5
Number of Residues4
Detailsbinding site for residue TRS A 405
ChainResidue
ATRP41
APHE65
AASP67
ASER69

site_idAC6
Number of Residues4
Detailsbinding site for residue ZN B 401
ChainResidue
BCYS107
BCYS110
BCYS136
BCYS139

site_idAC7
Number of Residues4
Detailsbinding site for residue ZN B 402
ChainResidue
BCYS90
BCYS93
BHIS115
BCYS118

site_idAC8
Number of Residues4
Detailsbinding site for residue ZN B 403
ChainResidue
BCYS189
BCYS191
BHIS212
BCYS215

site_idAC9
Number of Residues4
Detailsbinding site for residue ZN B 404
ChainResidue
BCYS204
BCYS207
BCYS234
BCYS237

site_idAD1
Number of Residues3
Detailsbinding site for residue TRS B 405
ChainResidue
BTYR47
BASP67
BPHE71

site_idAD2
Number of Residues4
Detailsbinding site for residue ZN E 401
ChainResidue
ECYS90
ECYS93
EHIS115
ECYS118

site_idAD3
Number of Residues4
Detailsbinding site for residue ZN E 402
ChainResidue
ECYS189
ECYS191
EHIS212
ECYS215

site_idAD4
Number of Residues4
Detailsbinding site for residue ZN E 403
ChainResidue
ECYS107
ECYS110
ECYS136
ECYS139

site_idAD5
Number of Residues4
Detailsbinding site for residue ZN E 404
ChainResidue
ECYS204
ECYS207
ECYS234
ECYS237

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 Residues165
DetailsZN_FING: PHD-type 1 => ECO:0000255|PROSITE-ProRule:PRU00146
ChainResidueDetails
AGLU87-ALA142
BGLU87-ALA142
EGLU87-ALA142

site_idSWS_FT_FI2
Number of Residues162
DetailsZN_FING: PHD-type 2 => ECO:0000255|PROSITE-ProRule:PRU00146
ChainResidueDetails
AGLN186-GLY240
BGLN186-GLY240
EGLN186-GLY240

222624

PDB entries from 2024-07-17

PDB statisticsPDBj update infoContact PDBjnumon