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5Y1Z

Crystal structure of ZMYND8 PHD-BROMO-PWWP tandem in complex with Drebrin ADF-H domain

Functional Information from GO Data
ChainGOidnamespacecontents
A0003779molecular_functionactin binding
B0003779molecular_functionactin binding
C0006355biological_processregulation of DNA-templated transcription
D0006355biological_processregulation of DNA-templated transcription
Functional Information from PDB Data
site_idAC1
Number of Residues3
Detailsbinding site for residue SO4 A 201
ChainResidue
APRO91
AASP92
CLYS233

site_idAC2
Number of Residues4
Detailsbinding site for residue ZN C 501
ChainResidue
CCYS91
CCYS94
CHIS111
CCYS114

site_idAC3
Number of Residues4
Detailsbinding site for residue ZN C 502
ChainResidue
CCYS274
CHIS278
CCYS255
CCYS258

site_idAC4
Number of Residues4
Detailsbinding site for residue ZN C 503
ChainResidue
CCYS103
CCYS106
CCYS127
CCYS130

site_idAC5
Number of Residues4
Detailsbinding site for residue SO4 C 504
ChainResidue
CARG354
CTYR362
CSO4505
CHOH608

site_idAC6
Number of Residues3
Detailsbinding site for residue SO4 C 505
ChainResidue
CARG354
CSO4504
DARG96

site_idAC7
Number of Residues2
Detailsbinding site for residue SO4 C 506
ChainResidue
CLYS284
CGLY287

site_idAC8
Number of Residues4
Detailsbinding site for residue ZN D 501
ChainResidue
DCYS103
DCYS106
DCYS127
DCYS130

site_idAC9
Number of Residues4
Detailsbinding site for residue ZN D 502
ChainResidue
DCYS91
DCYS94
DHIS111
DCYS114

site_idAD1
Number of Residues4
Detailsbinding site for residue ZN D 503
ChainResidue
DCYS255
DCYS258
DCYS274
DHIS278

site_idAD2
Number of Residues4
Detailsbinding site for residue SO4 D 504
ChainResidue
DASN250
DARG297
DARG313
DTRP315

site_idAD3
Number of Residues3
Detailsbinding site for residue SO4 D 505
ChainResidue
DLYS299
DASP300
DTRP315

site_idAD4
Number of Residues4
Detailsbinding site for residue GOL D 506
ChainResidue
CARG355
DGLN99
DHOH623
DHOH624

Functional Information from PROSITE/UniProt
site_idPS01359
Number of Residues40
DetailsZF_PHD_1 Zinc finger PHD-type signature. CwvChregqv.......................................LcCel..Cprv.YHakClrltsepegd...................................WfCpeC
ChainResidueDetails
CCYS91-CYS130

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues90
DetailsZN_FING: PHD-type => ECO:0000255|PROSITE-ProRule:PRU00146
ChainResidueDetails
CASP88-ILE133
DASP88-ILE133

site_idSWS_FT_FI2
Number of Residues22
DetailsBINDING: BINDING => ECO:0000269|PubMed:28966017, ECO:0007744|PDB:5Y1Z
ChainResidueDetails
CCYS91
CCYS258
CCYS274
DCYS91
DCYS94
DCYS103
DCYS106
DHIS111
DCYS114
DCYS127
DCYS130
CCYS94
DCYS255
DCYS258
DCYS274
CCYS103
CCYS106
CHIS111
CCYS114
CCYS127
CCYS130
CCYS255

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:20068231
ChainResidueDetails
CTHR404
DTHR404

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569
ChainResidueDetails
CSER406
DSER406

site_idSWS_FT_FI5
Number of Residues4
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733
ChainResidueDetails
CLYS390
DLYS390

237992

PDB entries from 2025-06-25

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