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6YXF

Cryogenic human adiponectin receptor 2 (ADIPOR2) with Gd-DO3 ligand 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
AOLA402

site_idAC2
Number of Residues12
Detailsbinding site for residue OLA A 402
ChainResidue
ATYR321
AALA325
ATYR328
AHIS348
APHE351
APHE354
AZN401
AASP219
ATYR220
AILE223
ALEU226
APHE282

site_idAC3
Number of Residues6
Detailsbinding site for residue OLB A 403
ChainResidue
ASER230
AGLY289
ALEU314
AMET315
ATYR321
AHIS362

site_idAC4
Number of Residues11
Detailsbinding site for residue OLB A 404
ChainResidue
AGLY163
AILE164
AMET167
APHE168
AARG169
APRO170
AASN171
ALYS181
AGLY276
AILE322
AOLB407

site_idAC5
Number of Residues6
Detailsbinding site for residue OLB A 405
ChainResidue
AVAL157
APHE158
ACYS161
AILE164
APHE165
APHE168

site_idAC6
Number of Residues4
Detailsbinding site for residue OLB A 406
ChainResidue
AGLN179
ALEU189
AVAL232
ATYR240

site_idAC7
Number of Residues7
Detailsbinding site for residue OLB A 407
ChainResidue
AASN171
APRO272
AGLN273
AGLY276
AARG331
AARG335
AOLB404

site_idAC8
Number of Residues1
Detailsbinding site for residue GD A 408
ChainResidue
ADO3410

site_idAC9
Number of Residues2
Detailsbinding site for residue GD A 409
ChainResidue
AGLU209
ADO3411

site_idAD1
Number of Residues5
Detailsbinding site for residue DO3 A 410
ChainResidue
AVAL105
AGD408
AHOH504
HGD302
HDO3303

site_idAD2
Number of Residues3
Detailsbinding site for residue DO3 A 411
ChainResidue
AGLU209
AARG213
AGD409

site_idAD3
Number of Residues11
Detailsbinding site for residue OLB H 301
ChainResidue
ASER131
APHE132
AARG133
APHE136
AGLY301
APHE302
ALEU303
HASN167
HHIS169
HASN170
HGLY207

site_idAD4
Number of Residues2
Detailsbinding site for residue GD H 302
ChainResidue
ADO3410
HDO3303

site_idAD5
Number of Residues4
Detailsbinding site for residue DO3 H 303
ChainResidue
ADO3410
HASN54
HSER55
HGD302

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 2024-10-30

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