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3O70

PHD-type zinc finger of human PHD finger protein 13

Functional Information from GO Data
ChainGOidnamespacecontents
A0016627molecular_functionoxidoreductase activity, acting on the CH-CH group of donors
A0050660molecular_functionflavin adenine dinucleotide binding
Functional Information from PDB Data
site_idAC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL A 400
ChainResidue
AHOH3
AHOH9
AHOH12
AGLU248
AASN250
AARG264
AGLU270
APHE272

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL A 401
ChainResidue
AHOH24
ATYR228
AMET246
AHOH16

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 500
ChainResidue
ACYS235
ACYS237
AHIS257
ACYS260

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 501
ChainResidue
ACYS249
ACYS252
ACYS274
ACYS277

Functional Information from PROSITE/UniProt
site_idPS01186
Number of Residues15
DetailsEGF_2 EGF-like domain signature 2. CfCmkPFagrpmie.C
ChainResidueDetails
ACYS235-CYS249

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues48
DetailsZinc finger: {"description":"PHD-type"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues7
DetailsRegion: {"description":"Interaction with trimethylated histone H3 (H3K4)","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"SEP-2010","submissionDatabase":"PDB data bank","title":"Crystal structure of PHF13 in complex with tri-methylated histone H3K4.","authoringGroup":["Structural genomics consortium (SGC)"]}},{"source":"PDB","id":"3O7A","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

248335

PDB entries from 2026-01-28

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