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3DZU

Intact PPAR gamma - RXR alpha Nuclear Receptor Complex on DNA bound with BVT.13, 9-cis Retinoic Acid and NCOA2 Peptide

Functional Information from GO Data
ChainGOidnamespacecontents
A0000122biological_processnegative regulation of transcription by RNA polymerase II
A0000785cellular_componentchromatin
A0000976molecular_functiontranscription cis-regulatory region binding
A0000977molecular_functionRNA polymerase II transcription regulatory region sequence-specific DNA binding
A0000978molecular_functionRNA polymerase II cis-regulatory region sequence-specific DNA binding
A0000981molecular_functionDNA-binding transcription factor activity, RNA polymerase II-specific
A0001221molecular_functiontranscription coregulator binding
A0001972molecular_functionretinoic acid binding
A0002157biological_processpositive regulation of thyroid hormone mediated signaling pathway
A0003677molecular_functionDNA binding
A0003690molecular_functiondouble-stranded DNA binding
A0003700molecular_functionDNA-binding transcription factor activity
A0003707molecular_functionnuclear steroid receptor activity
A0004879molecular_functionnuclear receptor activity
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005667cellular_componenttranscription regulator complex
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0005829cellular_componentcytosol
A0006355biological_processregulation of DNA-templated transcription
A0008270molecular_functionzinc ion binding
A0009755biological_processhormone-mediated signaling pathway
A0010875biological_processpositive regulation of cholesterol efflux
A0016922molecular_functionnuclear receptor binding
A0019899molecular_functionenzyme binding
A0030154biological_processcell differentiation
A0030501biological_processpositive regulation of bone mineralization
A0032411biological_processpositive regulation of transporter activity
A0032526biological_processresponse to retinoic acid
A0035357biological_processperoxisome proliferator activated receptor signaling pathway
A0042277molecular_functionpeptide binding
A0042789biological_processmRNA transcription by RNA polymerase II
A0042802molecular_functionidentical protein binding
A0042809molecular_functionnuclear vitamin D receptor binding
A0043167molecular_functionion binding
A0043235cellular_componentreceptor complex
A0043401biological_processsteroid hormone mediated signaling pathway
A0043565molecular_functionsequence-specific DNA binding
A0044323molecular_functionretinoic acid-responsive element binding
A0045893biological_processpositive regulation of DNA-templated transcription
A0045944biological_processpositive regulation of transcription by RNA polymerase II
A0046872molecular_functionmetal ion binding
A0048384biological_processretinoic acid receptor signaling pathway
A0050692molecular_functionDNA binding domain binding
A0050693molecular_functionLBD domain binding
A0070564biological_processpositive regulation of vitamin D receptor signaling pathway
A0070644molecular_functionvitamin D response element binding
A0090575cellular_componentRNA polymerase II transcription regulator complex
A1990837molecular_functionsequence-specific double-stranded DNA binding
D0003677molecular_functionDNA binding
D0003700molecular_functionDNA-binding transcription factor activity
D0004879molecular_functionnuclear receptor activity
D0005634cellular_componentnucleus
D0006355biological_processregulation of DNA-templated transcription
D0008270molecular_functionzinc ion binding
D0043565molecular_functionsequence-specific DNA binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN D 7121
ChainResidue
DCYS111
DCYS114
DCYS128
DCYS131

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN D 7122
ChainResidue
DCYS148
DLEU150
DCYS152
DCYS162
DCYS165

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 7221
ChainResidue
ACYS135
ACYS138
ACYS152
ACYS155

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 7222
ChainResidue
ACYS171
ACYS177
ACYS187
ACYS190

site_idAC5
Number of Residues11
DetailsBINDING SITE FOR RESIDUE 9CR A 7223
ChainResidue
AILE268
AALA271
AALA272
AGLN275
AASN306
AILE310
APHE313
AARG316
ALEU326
ACYS432
AHIS435

site_idAC6
Number of Residues9
DetailsBINDING SITE FOR RESIDUE PLB D 701
ChainResidue
DARG280
DILE281
DGLY284
DCYS285
DARG288
DLEU333
DLEU340
DILE341
DSER342

Functional Information from PROSITE/UniProt
site_idPS00031
Number of Residues27
DetailsNUCLEAR_REC_DBD_1 Nuclear hormones receptors DNA-binding region signature. CaiCg.Drssgk.HYgvysCegCkgFFkR
ChainResidueDetails
ACYS135-ARG161
DCYS111-ARG137

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues74
DetailsDNA_BIND: Nuclear receptor => ECO:0000255|PROSITE-ProRule:PRU00407
ChainResidueDetails
DALA108-PHE182

site_idSWS_FT_FI2
Number of Residues42
DetailsZN_FING: NR C4-type => ECO:0000255|PROSITE-ProRule:PRU00407
ChainResidueDetails
DCYS111-CYS131
DCYS148-CYS170

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:9744270, ECO:0007744|PDB:2PRG
ChainResidueDetails
DGLN286
DHIS323
DHIS449
DTYR473
ACYS171
ACYS177
ACYS187
ACYS190

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
DSER84
AALA327

site_idSWS_FT_FI5
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:36737649
ChainResidueDetails
DLYS224

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:11162439
ChainResidueDetails
ASER27

site_idSWS_FT_FI7
Number of Residues3
DetailsMOD_RES: Phosphoserine; by MAPK8 and MAPK9 => ECO:0000250|UniProtKB:P28700
ChainResidueDetails
ASER56
ASER70
ASER260

site_idSWS_FT_FI8
Number of Residues1
DetailsMOD_RES: Phosphothreonine; by MAPK8 and MAPK9 => ECO:0000250|UniProtKB:P28700
ChainResidueDetails
ATHR82

site_idSWS_FT_FI9
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER129

site_idSWS_FT_FI10
Number of Residues1
DetailsMOD_RES: N6-acetyllysine; by EP300 => ECO:0000269|PubMed:17761950
ChainResidueDetails
ALYS145

site_idSWS_FT_FI11
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569
ChainResidueDetails
ASER259

site_idSWS_FT_FI12
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) => ECO:0000269|PubMed:16912044
ChainResidueDetails
ALYS108

218196

PDB entries from 2024-04-10

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