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6KS1

Crystal structure of the human adiponectin receptor 2

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
AHOH501
AHOH522

site_idAC2
Number of Residues12
Detailsbinding site for residue OLA A 402
ChainResidue
ALEU320
ATYR321
ATYR328
APHE351
APHE354
AGLY358
AALA359
AHOH522
ATYR220
AARG278
AALA279
AMET317

site_idAC3
Number of Residues6
Detailsbinding site for residue OLB A 404
ChainResidue
ALEU189
ALEU193
ALYS217
ALEU218
AGLN265
AOLB406

site_idAC4
Number of Residues3
Detailsbinding site for residue OLB A 405
ChainResidue
ALEU193
ALEU214
AOLC408

site_idAC5
Number of Residues3
Detailsbinding site for residue OLB A 406
ChainResidue
AILE262
AGLN265
AOLB404

site_idAC6
Number of Residues7
Detailsbinding site for residue OLB A 407
ChainResidue
AMET167
APHE168
ALEU283
ALEU287
AILE322
AALA326
AOLB403

site_idAC7
Number of Residues4
Detailsbinding site for residue OLC A 408
ChainResidue
APHE197
ALEU200
APHE215
AOLB405

site_idAC8
Number of Residues16
Detailsbinding site for residues OLB A 403 and LPX A 409
ChainResidue
ASER131
APHE132
AARG133
APHE136
ACYS156
ALEU160
ATRP199
ALEU287
ALEU294
AVAL297
AGLY301
APHE302
AOLB407
AHOH503
LASN28
LHIS30

site_idAC9
Number of Residues16
Detailsbinding site for residues OLB A 403 and LPX A 409
ChainResidue
ASER131
APHE132
AARG133
APHE136
ACYS156
ALEU160
ATRP199
ALEU287
ALEU294
AVAL297
AGLY301
APHE302
AOLB407
AHOH503
LASN28
LHIS30

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

224201

PDB entries from 2024-08-28

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