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4LK9

Crystal Structure of MOZ double PHD finger histone H3 tail complex

Functional Information from GO Data
ChainGOidnamespacecontents
B0000786cellular_componentnucleosome
B0003677molecular_functionDNA binding
B0030527molecular_functionstructural constituent of chromatin
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 401
ChainResidue
ACYS281
ACYS284
ACYS307
ACYS310

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 402
ChainResidue
ACYS265
ACYS268
AHIS289
ACYS292

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 403
ChainResidue
ACYS212
AHIS238
ACYS241
ACYS209

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 404
ChainResidue
ACYS230
ACYS233
ACYS259
ACYS262

site_idAC5
Number of Residues28
DetailsBINDING SITE FOR CHAIN B OF HISTONE H3.1
ChainResidue
APHE211
ACYS241
ALEU242
ALYS243
AILE260
AGLU261
ALYS263
AGLN271
AALA275
AASP276
AMET278
ALEU279
APHE280
ACYS281
AASP282
AASP285
AMET300
AGLY303
AHOH527
AHOH545
AHOH600
BHOH102
BHOH103
BHOH104
BHOH105
BHOH106
BHOH107
BHOH109

Functional Information from PROSITE/UniProt
site_idPS00322
Number of Residues7
DetailsHISTONE_H3_1 Histone H3 signature 1. KAPRKQL
ChainResidueDetails
BLYS14-LEU20

site_idPS01359
Number of Residues81
DetailsZF_PHD_1 Zinc finger PHD-type signature. CadCgnsghpsclkfspeltvrvkalrwqciecktcsscrdqgknadnmLfCds..Cdrg.FHmeCcdppltrmpkgm.................................WiCqiC
ChainResidueDetails
ACYS230-CYS310

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsMOD_RES: Citrulline; alternate => ECO:0000269|PubMed:16567635
ChainResidueDetails
BARG2

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: Phosphothreonine; by HASPIN and VRK1 => ECO:0000269|PubMed:15681610, ECO:0000269|PubMed:16185088, ECO:0000269|PubMed:31527692
ChainResidueDetails
BTHR3

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: N6-methyllysine; alternate => ECO:0000269|PubMed:16267050, ECO:0000269|PubMed:16457588, ECO:0000269|PubMed:17194708
ChainResidueDetails
BLYS4

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: 5-glutamyl serotonin; alternate => ECO:0000269|PubMed:30867594
ChainResidueDetails
BGLN5

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphothreonine; by PKC => ECO:0000269|PubMed:20228790
ChainResidueDetails
BTHR6

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Symmetric dimethylarginine; by PRMT5; alternate => ECO:0000250|UniProtKB:P68433
ChainResidueDetails
BARG8

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: N6-methyllysine; alternate => ECO:0000269|PubMed:11242053, ECO:0000269|PubMed:16185088, ECO:0000269|PubMed:16267050, ECO:0000269|PubMed:16457588, ECO:0000269|PubMed:17194708
ChainResidueDetails
BLYS9

site_idSWS_FT_FI8
Number of Residues1
DetailsMOD_RES: Phosphoserine; alternate; by AURKB, AURKC, RPS6KA3, RPS6KA4 and RPS6KA5 => ECO:0000269|PubMed:10464286, ECO:0000269|PubMed:11856369, ECO:0000269|PubMed:12560483, ECO:0000269|PubMed:15681610, ECO:0000269|PubMed:16185088, ECO:0000269|PubMed:16457588
ChainResidueDetails
BSER10

site_idSWS_FT_FI9
Number of Residues1
DetailsMOD_RES: Phosphothreonine; by PKC and CHEK1 => ECO:0000269|PubMed:12560483, ECO:0000269|PubMed:18066052, ECO:0000269|PubMed:18243098, ECO:0000269|PubMed:22901803
ChainResidueDetails
BTHR11

site_idSWS_FT_FI10
Number of Residues1
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000269|PubMed:22389435
ChainResidueDetails
BLYS14

site_idSWS_FT_FI11
Number of Residues1
DetailsMOD_RES: Citrulline; alternate => ECO:0000269|PubMed:15345777, ECO:0000269|PubMed:16497732, ECO:0000269|PubMed:16567635
ChainResidueDetails
BARG17

site_idSWS_FT_FI12
Number of Residues1
DetailsMOD_RES: N6-methyllysine; alternate => ECO:0000269|PubMed:16267050, ECO:0000269|PubMed:17194708
ChainResidueDetails
BLYS18

site_idSWS_FT_FI13
Number of Residues1
DetailsLIPID: N6-decanoyllysine => ECO:0000269|PubMed:35939806
ChainResidueDetails
BLYS18

237735

PDB entries from 2025-06-18

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