Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

4IQR

Multi-Domain Organization of the HNF4alpha Nuclear Receptor Complex on DNA

Functional Information from GO Data
ChainGOidnamespacecontents
A0000978molecular_functionRNA polymerase II cis-regulatory region sequence-specific DNA binding
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
B0000978molecular_functionRNA polymerase II cis-regulatory region sequence-specific DNA binding
B0003677molecular_functionDNA binding
B0003700molecular_functionDNA-binding transcription factor activity
B0003707molecular_functionnuclear steroid receptor activity
B0005634cellular_componentnucleus
B0006355biological_processregulation of DNA-templated transcription
B0008270molecular_functionzinc ion binding
B0043565molecular_functionsequence-specific DNA binding
E0000978molecular_functionRNA polymerase II cis-regulatory region sequence-specific DNA binding
E0003677molecular_functionDNA binding
E0003700molecular_functionDNA-binding transcription factor activity
E0003707molecular_functionnuclear steroid receptor activity
E0005634cellular_componentnucleus
E0006355biological_processregulation of DNA-templated transcription
E0008270molecular_functionzinc ion binding
E0043565molecular_functionsequence-specific DNA binding
F0000978molecular_functionRNA polymerase II cis-regulatory region sequence-specific DNA binding
F0003677molecular_functionDNA binding
F0003700molecular_functionDNA-binding transcription factor activity
F0003707molecular_functionnuclear steroid receptor activity
F0005634cellular_componentnucleus
F0006355biological_processregulation of DNA-templated transcription
F0008270molecular_functionzinc ion binding
F0043565molecular_functionsequence-specific DNA binding
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MYR A 401
ChainResidue
ASER181
AGLN185
AARG226
ALEU236
AGLY237
AMET252
AGLN345

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 402
ChainResidue
ACYS68
ACYS71
ACYS51
ACYS54

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 403
ChainResidue
ACYS87
ACYS93
ACYS103
ACYS106

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MYR B 401
ChainResidue
BVAL178
BSER181
BGLN185
BARG226
BLEU236
BGLY237
BMET252

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 402
ChainResidue
BCYS51
BCYS54
BCYS68
BCYS71

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 403
ChainResidue
BCYS87
BCYS93
BCYS103
BCYS106

site_idAC7
Number of Residues10
DetailsBINDING SITE FOR RESIDUE MYR E 401
ChainResidue
EVAL178
ESER181
EMET182
EGLN185
EARG226
ELEU236
EGLY237
EMET252
ESER256
EILE259

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN E 402
ChainResidue
ECYS51
ECYS54
ECYS68
ECYS71

site_idAC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN E 403
ChainResidue
ECYS87
ECYS93
ECYS103
ECYS106

site_idBC1
Number of Residues9
DetailsBINDING SITE FOR RESIDUE MYR F 401
ChainResidue
FSER181
FGLN185
FALA223
FARG226
FMET252
FVAL255
FSER256
FILE259
FILE346

site_idBC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN F 402
ChainResidue
FCYS51
FCYS54
FCYS68
FCYS71

site_idBC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN F 403
ChainResidue
FCYS87
FCYS93
FCYS103
FCYS106

Functional Information from PROSITE/UniProt
site_idPS00031
Number of Residues27
DetailsNUCLEAR_REC_DBD_1 Nuclear hormones receptors DNA-binding region signature. CaiCg.Dratgk.HYgassCdgCkgFFrR
ChainResidueDetails
ACYS51-ARG77

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues300
DetailsDNA_BIND: Nuclear receptor => ECO:0000255|PROSITE-ProRule:PRU00407
ChainResidueDetails
ASER48-ASN123
BSER48-ASN123
ESER48-ASN123
FSER48-ASN123

site_idSWS_FT_FI2
Number of Residues176
DetailsZN_FING: NR C4-type => ECO:0000255|PROSITE-ProRule:PRU00407
ChainResidueDetails
ACYS51-CYS71
ACYS87-CYS111
BCYS51-CYS71
BCYS87-CYS111
ECYS51-CYS71
ECYS87-CYS111
FCYS51-CYS71
FCYS87-CYS111

site_idSWS_FT_FI3
Number of Residues8
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:21708125
ChainResidueDetails
ASER133
ASER158
BSER133
BSER158
ESER133
ESER158
FSER133
FSER158

site_idSWS_FT_FI4
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P22449
ChainResidueDetails
ASER134
BSER134
ESER134
FSER134

site_idSWS_FT_FI5
Number of Residues4
DetailsMOD_RES: Phosphotyrosine => ECO:0007744|PubMed:24275569
ChainResidueDetails
ATYR135
BTYR135
ETYR135
FTYR135

site_idSWS_FT_FI6
Number of Residues4
DetailsMOD_RES: Phosphothreonine => ECO:0000269|PubMed:21708125
ChainResidueDetails
ATHR157
BTHR157
ETHR157
FTHR157

site_idSWS_FT_FI7
Number of Residues4
DetailsMOD_RES: Phosphoserine; by AMPK => ECO:0000269|PubMed:12740371
ChainResidueDetails
ASER304
BSER304
ESER304
FSER304

site_idSWS_FT_FI8
Number of Residues12
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:21708125
ChainResidueDetails
ALYS225
FLYS225
FLYS298
ALYS298
BLYS225
BLYS298
ELYS225
ELYS298

218853

PDB entries from 2024-04-24

PDB statisticsPDBj update infoContact PDBjnumon