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5LWY

Revised crystal structure of the human adiponectin receptor 2 in complex with a C18 free fatty acid

Replaces:  3WXW
Functional Information from GO Data
ChainGOidnamespacecontents
A0016020cellular_componentmembrane
Functional Information from PDB Data
site_idAC1
Number of Residues5
Detailsbinding site for residue ZN A 401
ChainResidue
AHIS202
AHIS348
AHIS352
AHOH503
AHOH537

site_idAC2
Number of Residues11
Detailsbinding site for residue OLB A 402
ChainResidue
APHE302
ALEU303
AOLB404
AHOH502
AHOH511
LASN28
LHIS30
APHE132
AARG133
AVAL297
AGLY301

site_idAC3
Number of Residues3
Detailsbinding site for residue OLB A 403
ChainResidue
APHE197
AOLB404
AOLB406

site_idAC4
Number of Residues4
Detailsbinding site for residue OLB A 404
ChainResidue
ATRP199
AOLB402
AOLB403
AOLB409

site_idAC5
Number of Residues3
Detailsbinding site for residue OLB A 405
ChainResidue
ALYS217
ALEU225
AGLN265

site_idAC6
Number of Residues1
Detailsbinding site for residue OLB A 406
ChainResidue
AOLB403

site_idAC7
Number of Residues4
Detailsbinding site for residue OLB A 407
ChainResidue
AMET228
ACYS254
AILE262
AGLN265

site_idAC8
Number of Residues7
Detailsbinding site for residue OLB A 408
ChainResidue
AILE164
AMET167
APHE168
AGLY276
ALEU283
ALEU287
AILE322

site_idAC9
Number of Residues9
Detailsbinding site for residue OLB A 409
ChainResidue
AGLY286
AGLY289
AILE290
APHE302
AILE311
ALEU314
AMET317
AHIS362
AOLB404

site_idAD1
Number of Residues17
Detailsbinding site for residue OLA A 410
ChainResidue
ATYR220
AILE223
AARG278
AALA279
APHE282
ALEU283
AMET317
ALEU320
ATYR321
AALA325
ATYR328
APHE351
APHE354
AVAL355
AGLY358
AHOH503
AHOH537

site_idAD2
Number of Residues3
Detailsbinding site for residue GOL L 201
ChainResidue
LGLN37
LLEU47
LGLY57

Functional Information from PROSITE/UniProt
site_idPS00213
Number of Residues12
DetailsLIPOCALIN Lipocalin signature. GGS..EFEGRWRVI
ChainResidueDetails
AGLY-4-ILE106

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues20
DetailsTRANSMEM: Helical; Name=1 => ECO:0000269|PubMed:25855295
ChainResidueDetails
AASN148-PHE168

site_idSWS_FT_FI2
Number of Residues52
DetailsTOPO_DOM: Extracellular => ECO:0000269|PubMed:25855295
ChainResidueDetails
AARG169-LYS181
ALEU235-PRO245
AHIS295-GLY309
AGLN370-LEU386

site_idSWS_FT_FI3
Number of Residues20
DetailsTRANSMEM: Helical; Name=2 => ECO:0000269|PubMed:25855295
ChainResidueDetails
AVAL182-HIS202

site_idSWS_FT_FI4
Number of Residues33
DetailsTOPO_DOM: Cytoplasmic => ECO:0000269|PubMed:25855295
ChainResidueDetails
ATHR203-ARG213
AASP267-GLN273
AARG331-HIS348

site_idSWS_FT_FI5
Number of Residues20
DetailsTRANSMEM: Helical; Name=3 => ECO:0000269|PubMed:25855295
ChainResidueDetails
ALEU214-TRP234

site_idSWS_FT_FI6
Number of Residues20
DetailsTRANSMEM: Helical; Name=4 => ECO:0000269|PubMed:25855295
ChainResidueDetails
ACYS246-TRP266

site_idSWS_FT_FI7
Number of Residues20
DetailsTRANSMEM: Helical; Name=5 => ECO:0000269|PubMed:25855295
ChainResidueDetails
ATYR274-LEU294

site_idSWS_FT_FI8
Number of Residues20
DetailsTRANSMEM: Helical; Name=6 => ECO:0000269|PubMed:25855295
ChainResidueDetails
AGLN310-ALA330

site_idSWS_FT_FI9
Number of Residues20
DetailsTRANSMEM: Helical; Name=7 => ECO:0000269|PubMed:25855295
ChainResidueDetails
AGLN349-LEU369

site_idSWS_FT_FI10
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:25855295
ChainResidueDetails
AHIS202
AHIS348
AHIS352

219140

PDB entries from 2024-05-01

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