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2KWK

Solution structures of the double PHD fingers of human transcriptional protein DPF3b bound to a H3 peptide wild type

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 Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 501
ChainResidue
ACYS262
ACYS265
AASN272
AHIS292
ACYS295

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 601
ChainResidue
ACYS284
ACYS287
ACYS313
ACYS316

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 701
ChainResidue
ACYS334
ACYS337
ACYS360
ACYS363

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 801
ChainResidue
ACYS319
ACYS322
AHIS342
ACYS345

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 Residues80
DetailsZF_PHD_1 Zinc finger PHD-type signature. CadCgrsghptclqftlnmteavktykwqcieckscilcgtsenddql.LfCdd..Cdrg.YHmyClnppvaeppegs.................................WsChlC
ChainResidueDetails
ACYS284-CYS363

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

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PDB entries from 2024-07-24

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