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5XFR

Ternary complex of MTF2, DNA and histone

Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue ZN A 401
ChainResidue
ACYS105
ACYS108
AHIS130
ACYS133

site_idAC2
Number of Residues4
Detailsbinding site for residue ZN A 402
ChainResidue
ACYS122
ACYS125
ACYS151
ACYS154

site_idAC3
Number of Residues4
Detailsbinding site for residue ZN A 403
ChainResidue
ACYS222
ACYS249
ACYS252
ACYS219

site_idAC4
Number of Residues4
Detailsbinding site for residue ZN A 404
ChainResidue
ACYS204
ACYS206
AHIS227
ACYS230

site_idAC5
Number of Residues4
Detailsbinding site for residue ZN B 401
ChainResidue
BCYS122
BCYS125
BCYS151
BCYS154

site_idAC6
Number of Residues4
Detailsbinding site for residue ZN B 402
ChainResidue
BCYS105
BCYS108
BHIS130
BCYS133

site_idAC7
Number of Residues4
Detailsbinding site for residue ZN B 403
ChainResidue
BCYS204
BCYS206
BHIS227
BCYS230

site_idAC8
Number of Residues4
Detailsbinding site for residue ZN B 404
ChainResidue
BCYS219
BCYS222
BCYS249
BCYS252

Functional Information from PROSITE/UniProt
site_idPS01359
Number of Residues50
DetailsZF_PHD_1 Zinc finger PHD-type signature. CtiCqeeyseapnem..................................ViCdk..Cgqg.YHqlChtphidcsvidsdek..............................WlCrqC
ChainResidueDetails
ACYS105-CYS154
ACYS202-CYS252

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsMOD_RES: N6-methyllysine; alternate => ECO:0000269|PubMed:15983376, ECO:0000269|PubMed:16185088, ECO:0000269|PubMed:16267050, ECO:0000269|PubMed:16627869, ECO:0000269|PubMed:17194708
ChainResidueDetails
CM3L36
DM3L36

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: N6-methyllysine => ECO:0000269|PubMed:15983376
ChainResidueDetails
CLYS37
DLYS37

223166

PDB entries from 2024-07-31

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