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4NQA

Crystal structure of liganded hRXR-alpha/hLXR-beta heterodimer on DNA

Functional Information from GO Data
ChainGOidnamespacecontents
A0003677molecular_functionDNA binding
A0003700molecular_functionDNA-binding transcription factor activity
A0003707molecular_functionnuclear steroid receptor activity
A0005634cellular_componentnucleus
A0006355biological_processregulation of DNA-templated transcription
A0008270molecular_functionzinc ion binding
A0043565molecular_functionsequence-specific DNA binding
B0003677molecular_functionDNA binding
B0003700molecular_functionDNA-binding transcription factor activity
B0004879molecular_functionnuclear receptor activity
B0006355biological_processregulation of DNA-templated transcription
B0006629biological_processlipid metabolic process
B0008270molecular_functionzinc ion binding
B0043565molecular_functionsequence-specific DNA binding
H0003677molecular_functionDNA binding
H0003700molecular_functionDNA-binding transcription factor activity
H0003707molecular_functionnuclear steroid receptor activity
H0005634cellular_componentnucleus
H0006355biological_processregulation of DNA-templated transcription
H0008270molecular_functionzinc ion binding
H0043565molecular_functionsequence-specific DNA binding
I0003677molecular_functionDNA binding
I0003700molecular_functionDNA-binding transcription factor activity
I0004879molecular_functionnuclear receptor activity
I0006355biological_processregulation of DNA-templated transcription
I0006629biological_processlipid metabolic process
I0008270molecular_functionzinc ion binding
I0043565molecular_functionsequence-specific DNA binding
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE 9CR A 501
ChainResidue
AILE268
AGLN275
APHE313
AARG316
AALA327
ACYS432
AHIS435

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 502
ChainResidue
ACYS152
ACYS155
AARG184
ACYS135
ACYS138

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 503
ChainResidue
ACYS171
ACYS177
ACYS187
ACYS190

site_idAC4
Number of Residues15
DetailsBINDING SITE FOR RESIDUE 965 B 501
ChainResidue
BPHE271
BLEU274
BALA275
BSER278
BILE309
BMET312
BLEU313
BTHR316
BARG319
BPHE329
BLEU330
BPHE340
BPHE354
BHIS435
BTRP457

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 502
ChainResidue
BCYS87
BCYS90
BCYS104
BCYS107

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 503
ChainResidue
BCYS125
BCYS131
BCYS141
BCYS144

site_idAC7
Number of Residues8
DetailsBINDING SITE FOR RESIDUE 9CR H 501
ChainResidue
HALA271
HGLN275
HPHE313
HARG316
HLEU326
HALA327
HILE345
HCYS432

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN H 502
ChainResidue
HCYS135
HCYS138
HCYS152
HCYS155

site_idAC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN H 503
ChainResidue
HCYS171
HCYS177
HCYS187
HCYS190

site_idBC1
Number of Residues19
DetailsBINDING SITE FOR RESIDUE 965 I 501
ChainResidue
IPHE271
ILEU274
IALA275
ISER278
IGLU281
IMET312
ILEU313
ITHR316
IARG319
IPHE329
ILEU330
IPHE340
ILEU345
IPHE349
IILE350
IILE353
IPHE354
IHIS435
ITRP457

site_idBC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN I 502
ChainResidue
ICYS87
ICYS90
ICYS104
ICYS107

site_idBC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN I 503
ChainResidue
ICYS125
ICYS131
ICYS141
ICYS144

Functional Information from PROSITE/UniProt
site_idPS00031
Number of Residues27
DetailsNUCLEAR_REC_DBD_1 Nuclear hormones receptors DNA-binding region signature. CrvCg.Dkasgf.HYnvlsCegCkgFFrR
ChainResidueDetails
BCYS87-ARG113
ACYS135-ARG161

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues154
DetailsDNA_BIND: Nuclear receptor => ECO:0000255|PROSITE-ProRule:PRU00407
ChainResidueDetails
BHIS84-SER161
IHIS84-SER161

site_idSWS_FT_FI2
Number of Residues88
DetailsZN_FING: NR C4-type => ECO:0000255|PROSITE-ProRule:PRU00407
ChainResidueDetails
BCYS87-CYS107
BCYS125-CYS149
ICYS87-CYS107
ICYS125-CYS149

site_idSWS_FT_FI3
Number of Residues6
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0000269|PubMed:20159957
ChainResidueDetails
BLYS410
HCYS138
HCYS152
HCYS155
HCYS171
HCYS177
HCYS187
HCYS190
ACYS138
BLYS448
ILYS410
ACYS171
ILYS448
ACYS187
ACYS190
HCYS135

site_idSWS_FT_FI4
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:16107141, ECO:0000269|PubMed:18800767, ECO:0000269|PubMed:19167885, ECO:0007744|PDB:2ACL, ECO:0007744|PDB:3FAL, ECO:0007744|PDB:3FC6
ChainResidueDetails
AARG316
AALA327
HARG316
HALA327

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER129
HSER129

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: N6-acetyllysine; by EP300 => ECO:0000269|PubMed:17761950
ChainResidueDetails
ALYS145
HLYS145

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569
ChainResidueDetails
ASER259
HSER259

site_idSWS_FT_FI8
Number of Residues2
DetailsMOD_RES: Phosphoserine; by MAPK8 and MAPK9 => ECO:0000250|UniProtKB:P28700
ChainResidueDetails
ASER260
HSER260

site_idSWS_FT_FI9
Number of Residues4
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) => ECO:0000269|PubMed:16912044
ChainResidueDetails
ALYS108
HLYS108

224201

PDB entries from 2024-08-28

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