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4O9S

Crystal structure of Retinol-Binding Protein 4 (RBP4)in complex with a non-retinoid ligand

Functional Information from GO Data
ChainGOidnamespacecontents
A0001654biological_processeye development
A0002639biological_processpositive regulation of immunoglobulin production
A0005501molecular_functionretinoid binding
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0006094biological_processgluconeogenesis
A0007507biological_processheart development
A0007601biological_processvisual perception
A0016918molecular_functionretinal binding
A0019841molecular_functionretinol binding
A0030277biological_processmaintenance of gastrointestinal epithelium
A0030324biological_processlung development
A0032024biological_processpositive regulation of insulin secretion
A0032526biological_processresponse to retinoic acid
A0034632molecular_functionretinol transmembrane transporter activity
A0034633biological_processretinol transport
A0042572biological_processretinol metabolic process
A0042593biological_processglucose homeostasis
A0048562biological_processembryonic organ morphogenesis
A0048706biological_processembryonic skeletal system development
A0048738biological_processcardiac muscle tissue development
A0048807biological_processfemale genitalia morphogenesis
A0060044biological_processnegative regulation of cardiac muscle cell proliferation
A0060059biological_processembryonic retina morphogenesis in camera-type eye
A0060065biological_processuterus development
A0060068biological_processvagina development
A0060157biological_processurinary bladder development
A0060347biological_processheart trabecula formation
A0070062cellular_componentextracellular exosome
B0001654biological_processeye development
B0002639biological_processpositive regulation of immunoglobulin production
B0005501molecular_functionretinoid binding
B0005515molecular_functionprotein binding
B0005576cellular_componentextracellular region
B0005615cellular_componentextracellular space
B0006094biological_processgluconeogenesis
B0007507biological_processheart development
B0007601biological_processvisual perception
B0016918molecular_functionretinal binding
B0019841molecular_functionretinol binding
B0030277biological_processmaintenance of gastrointestinal epithelium
B0030324biological_processlung development
B0032024biological_processpositive regulation of insulin secretion
B0032526biological_processresponse to retinoic acid
B0034632molecular_functionretinol transmembrane transporter activity
B0034633biological_processretinol transport
B0042572biological_processretinol metabolic process
B0042593biological_processglucose homeostasis
B0048562biological_processembryonic organ morphogenesis
B0048706biological_processembryonic skeletal system development
B0048738biological_processcardiac muscle tissue development
B0048807biological_processfemale genitalia morphogenesis
B0060044biological_processnegative regulation of cardiac muscle cell proliferation
B0060059biological_processembryonic retina morphogenesis in camera-type eye
B0060065biological_processuterus development
B0060068biological_processvagina development
B0060157biological_processurinary bladder development
B0060347biological_processheart trabecula formation
B0070062cellular_componentextracellular exosome
Functional Information from PDB Data
site_idAC1
Number of Residues15
DetailsBINDING SITE FOR RESIDUE 2RY A 201
ChainResidue
ALEU35
ATYR90
AASP102
AARG121
ATYR133
APHE135
AHOH303
APHE36
ALEU37
AALA55
AALA57
AMET73
AVAL74
AGLY75
AMET88

site_idAC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE EDO A 202
ChainResidue
AGLU81
AASP82

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO A 203
ChainResidue
APHE9
AARG10
AVAL107
AARG155
AGLU158
AEDO211

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO A 204
ChainResidue
AASP126
ALEU144
AHOH311

site_idAC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE EDO A 205
ChainResidue
ATHR80
AGLU81

site_idAC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO A 206
ChainResidue
AGLN156
AARG163
ATYR165

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 207
ChainResidue
AVAL42
ATHR56
AALA57
ALYS58

site_idAC8
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO A 208
ChainResidue
AASP31
AGLN164
AARG166

site_idAC9
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO A 209
ChainResidue
ALYS30
AASP31
APRO32
AGLU33
AALA130
AASP131
ASER132

site_idBC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 210
ChainResidue
AVAL42
AHIS170
AASN171
AGLY172

site_idBC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO A 211
ChainResidue
AARG10
AVAL11
AVAL107
AARG155
AEDO203
AHOH313

site_idBC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 212
ChainResidue
AASN142
AHIS170
APEG217
AHOH354

site_idBC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 213
ChainResidue
AASN66
ATRP67
BLEU35
B2RY201

site_idBC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 214
ChainResidue
ATRP91
BTRP91
BEDO209
BHOH398

site_idBC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL A 215
ChainResidue
AASP72
AALA94
ASER95
APHE96

site_idBC7
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CL A 216
ChainResidue
BTRP67

site_idBC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PEG A 217
ChainResidue
AASP103
ACYS120
AHIS170
AASN171
AEDO212
AHOH400

site_idBC9
Number of Residues17
DetailsBINDING SITE FOR RESIDUE 2RY B 201
ChainResidue
AEDO213
BLEU35
BPHE36
BLEU37
BALA55
BALA57
BVAL61
BMET73
BVAL74
BGLY75
BMET88
BTYR90
BASP102
BARG121
BTYR133
BPHE135
BHOH307

site_idCC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO B 202
ChainResidue
AGLU13
AASN14
BPRO145
BGLU147

site_idCC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO B 203
ChainResidue
BPHE9
BARG10
BVAL107
BARG155
BGLU158

site_idCC3
Number of Residues1
DetailsBINDING SITE FOR RESIDUE EDO B 204
ChainResidue
BASP3

site_idCC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO B 205
ChainResidue
BARG10
BVAL11
BLYS12
BVAL107
BASP108
BARG155
BHOH318

site_idCC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO B 206
ChainResidue
BASP103
BCYS120
BLEU123
BVAL169
BHIS170
BEDO210
BEDO214

site_idCC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO B 207
ChainResidue
BLYS30
BASP31
BGLN164
BHOH394

site_idCC7
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO B 208
ChainResidue
BLYS87
BASN101
BASP102
BASP103
BASN171
BEDO213
BEDO214

site_idCC8
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO B 209
ChainResidue
ALEU97
AEDO214
BTRP91
BGLY92
BLEU97
BGLN98
BHOH341

site_idCC9
Number of Residues8
DetailsBINDING SITE FOR RESIDUE EDO B 210
ChainResidue
BLEU123
BPRO141
BASN142
BHIS170
BEDO206
BEDO214
BHOH368
BHOH411

site_idDC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO B 212
ChainResidue
BARG153
BGLN156
BARG163
BGLN164
BTYR165
BHOH326

site_idDC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO B 213
ChainResidue
BASN101
BASP102
BARG121
BVAL169
BASN171
BEDO208
BHOH343

site_idDC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO B 214
ChainResidue
BLYS87
BASP103
BHIS170
BASN171
BEDO206
BEDO208
BEDO210

site_idDC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL B 215
ChainResidue
BASP72
BALA94
BSER95
BPHE96

Functional Information from PROSITE/UniProt
site_idPS00213
Number of Residues14
DetailsLIPOCALIN Lipocalin signature. NFDkaRFSGTWYAM
ChainResidueDetails
AASN14-MET27

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P27485
ChainResidueDetails
AGLN98
BGLN98

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: Omega-N-methylarginine => ECO:0000250|UniProtKB:Q00724
ChainResidueDetails
AARG121
BARG121

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PDB entries from 2024-07-10

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