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6YX9

Cryogenic human adiponectin receptor 2 (ADIPOR2) at 2.4 A resolution determined by Serial Crystallography (SSX) using CrystalDirect

Functional Information from GO Data
ChainGOidnamespacecontents
A0016020cellular_componentmembrane
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue ZN A 401
ChainResidue
AHIS202
AHIS348
AHIS352
AOLA407

site_idAC2
Number of Residues14
Detailsbinding site for residue OLB A 402
ChainResidue
AVAL297
AILE298
APHE302
ALEU303
AHOH501
LASN28
LHIS30
LASN31
LGLY68
ASER131
APHE132
AARG133
APHE136
ALEU200

site_idAC3
Number of Residues6
Detailsbinding site for residue OLB A 403
ChainResidue
ALEU154
APHE158
ACYS161
APHE165
APHE168
AARG169

site_idAC4
Number of Residues6
Detailsbinding site for residue OLB A 404
ChainResidue
ALEU214
ALYS217
ALEU218
ASER221
ALEU225
AGLN265

site_idAC5
Number of Residues12
Detailsbinding site for residue OLB A 405
ChainResidue
AMET167
APHE168
AARG169
AASN171
APRO272
AGLN273
AARG275
AILE322
AALA329
AARG331
AARG335
AHOH506

site_idAC6
Number of Residues10
Detailsbinding site for residue OLB A 406
ChainResidue
ASER230
AGLY286
AILE290
APHE302
AILE311
ALEU314
AMET317
ATYR321
AHIS362
AOLA407

site_idAC7
Number of Residues13
Detailsbinding site for residue OLA A 407
ChainResidue
AASP219
AILE223
APHE282
ALEU320
ATYR321
ATYR328
AHIS348
APHE351
APHE354
AGLY358
AZN401
AOLB406
AHOH502

site_idAC8
Number of Residues4
Detailsbinding site for residue GOL L 201
ChainResidue
LGLN37
LGLN45
LPHE62
LASP82

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

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PDB entries from 2024-07-24

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