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4PSQ

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 Residues9
DetailsBINDING SITE FOR RESIDUE 2WL B 201
ChainResidue
AASN66
ATRP67
BPHE36
BLEU37
BMET73
BMET88
BTYR90
BGLY100
BARG121

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PO4 B 202
ChainResidue
BLYS12
BARG19
BTYR111
BHOH353

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO B 203
ChainResidue
BPHE9
BARG10
BVAL107
BARG155
BGLU158

site_idAC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE EDO B 204
ChainResidue
BSER7
BLYS85

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO B 205
ChainResidue
BARG153
BALA162
BARG163
BGLN164
BTYR165

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO B 206
ChainResidue
BASP103
BCYS120
BVAL169
BHIS170
BASN171
BHOH351

site_idAC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO B 208
ChainResidue
BARG166
BLEU167
BHOH365

site_idAC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO B 209
ChainResidue
BARG5
BASP126
BASP140
BGLY143
BLEU144

site_idAC9
Number of Residues9
DetailsBINDING SITE FOR RESIDUE EDO B 210
ChainResidue
BASP108
BTHR109
BASP110
BTYR114
BILE151
BARG155
BHOH353
BHOH360
BHOH367

site_idBC1
Number of Residues9
DetailsBINDING SITE FOR RESIDUE 2WL A 201
ChainResidue
ALEU35
APHE36
ALEU37
AMET88
ATYR90
AGLY100
AARG121
BASN66
BTRP67

site_idBC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE PO4 A 202
ChainResidue
ALYS12
AARG19
ATYR111

site_idBC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 203
ChainResidue
AARG153
AGLN156
AARG163
AGLN164
ATYR165

site_idBC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 204
ChainResidue
AASP103
ACYS120
AHIS170
AHOH348
AHOH354

site_idBC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO A 205
ChainResidue
APHE9
AARG10
AVAL107
AARG155
AGLU158
AEDO213

site_idBC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 206
ChainResidue
AARG5
AASP126
AGLY143
ALEU144

site_idBC7
Number of Residues2
DetailsBINDING SITE FOR RESIDUE EDO A 207
ChainResidue
AARG163
AARG166

site_idBC8
Number of Residues8
DetailsBINDING SITE FOR RESIDUE EDO A 208
ChainResidue
ATRP67
AASP68
AVAL69
ACYS70
BASP72
BGLY92
BVAL93
BALA94

site_idBC9
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 209
ChainResidue
ACYS129
ASER132
ALEU161
AGLN164
AHOH355

site_idCC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO A 210
ChainResidue
ALYS99
BLYS89
BLYS99

site_idCC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO A 211
ChainResidue
ALYS85
ATRP105
ASER7

site_idCC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 212
ChainResidue
ALYS29
ALYS30
AASP31
AGLN164
AARG166

site_idCC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 213
ChainResidue
AVAL11
AVAL107
AASP108
AARG155
AEDO205

site_idCC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO A 214
ChainResidue
AVAL42
ATHR56
ALYS58

Functional Information from PROSITE/UniProt
site_idPS00213
Number of Residues14
DetailsLIPOCALIN Lipocalin signature. NFDkaRFSGTWYAM
ChainResidueDetails
BASN14-MET27

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

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

222415

PDB entries from 2024-07-10

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