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6QBA

Crystal Structure of Retinol-Binding Protein 4 (RBP4) in complex with non-retinoid ligand A1120 and engineered binding scaffold

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
B0003677molecular_functionDNA binding
B0004519molecular_functionendonuclease activity
B0004521molecular_functionRNA endonuclease activity
Functional Information from PDB Data
site_idAC1
Number of Residues14
Detailsbinding site for residue 2T1 A 201
ChainResidue
ALEU35
APHE135
AHOH336
AHOH348
AHOH390
BTYR25
APHE36
ALEU37
AALA57
AMET73
AMET88
ATYR90
AHIS104
AARG121

site_idAC2
Number of Residues9
Detailsbinding site for residue IMD A 202
ChainResidue
AARG10
AVAL11
AGLU13
AVAL107
AARG155
AGLU158
AIMD205
AZN209
BGLU10

site_idAC3
Number of Residues6
Detailsbinding site for residue IMD A 203
ChainResidue
AASP140
AGLY143
AZN208
BGLU59
BHOH204
BHOH213

site_idAC4
Number of Residues7
Detailsbinding site for residue IMD A 204
ChainResidue
ATYR25
AHIS170
AASP175
AIMD206
AZN210
AHOH439
BGLN56

site_idAC5
Number of Residues7
Detailsbinding site for residue IMD A 205
ChainResidue
ALYS12
AGLU13
AASP108
AARG155
AIMD202
AZN209
BGLU10

site_idAC6
Number of Residues6
Detailsbinding site for residue IMD A 206
ChainResidue
AHIS170
AGLY172
AASP175
AIMD204
AZN210
BGLN56

site_idAC7
Number of Residues5
Detailsbinding site for residue PEG A 207
ChainResidue
AALA28
AGLN156
ATYR165
AHOH327
BGLU35

site_idAC8
Number of Residues6
Detailsbinding site for residue ZN A 208
ChainResidue
AASP140
AIMD203
BARG24
BGLU59
BHOH204
BHOH247

site_idAC9
Number of Residues4
Detailsbinding site for residue ZN A 209
ChainResidue
AGLU13
AIMD202
AIMD205
BGLU10

site_idAD1
Number of Residues4
Detailsbinding site for residue ZN A 210
ChainResidue
AHIS170
AASP175
AIMD204
AIMD206

site_idAD2
Number of Residues3
Detailsbinding site for residue ACT B 101
ChainResidue
BGLU53
BHOH214
BHOH227

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
DetailsMOD_RES: N6-methyllysine; partial => ECO:0000269|PubMed:8425540
ChainResidueDetails
BLYS4
BTHR6

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: Omega-N-methylarginine => ECO:0000250|UniProtKB:Q00724
ChainResidueDetails
AARG121

221716

PDB entries from 2024-06-26

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