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5B73

Crystal structure of human ZMYND8 PHD-Bromo-PWWP domain

Functional Information from GO Data
ChainGOidnamespacecontents
A0006355biological_processregulation of DNA-templated transcription
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue ZN A 501
ChainResidue
ACYS275
ACYS278
ACYS294
AHIS298

site_idAC2
Number of Residues4
Detailsbinding site for residue ZN A 502
ChainResidue
ACYS111
ACYS114
AHIS131
ACYS134

site_idAC3
Number of Residues4
Detailsbinding site for residue ZN A 503
ChainResidue
ACYS126
ACYS147
ACYS150
ACYS123

Functional Information from PROSITE/UniProt
site_idPS01359
Number of Residues40
DetailsZF_PHD_1 Zinc finger PHD-type signature. CwvChregqv.......................................LcCel..Cprv.YHakClrltsepegd...................................WfCpeC
ChainResidueDetails
ACYS111-CYS150

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues45
DetailsZN_FING: PHD-type => ECO:0000255|PROSITE-ProRule:PRU00146
ChainResidueDetails
AASP108-ILE153

site_idSWS_FT_FI2
Number of Residues11
DetailsBINDING: BINDING => ECO:0000269|PubMed:28966017, ECO:0007744|PDB:5Y1Z
ChainResidueDetails
ACYS111
ACYS278
ACYS294
ACYS114
ACYS123
ACYS126
AHIS131
ACYS134
ACYS147
ACYS150
ACYS275

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:20068231
ChainResidueDetails
ATHR424

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569
ChainResidueDetails
ASER426

site_idSWS_FT_FI5
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733
ChainResidueDetails
ALYS410

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PDB entries from 2024-09-11

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