6YXD

Room temperature structure of human adiponectin receptor 2 (ADIPOR2) at 2.9 A resolution determined by Serial Crystallography (SSX) using CrystalDirect

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0016020	cellular_component	membrane

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	binding site for residue ZN A 401

Chain	Residue
A	SER198
A	HIS202
A	HIS348
A	HIS352
A	HOH501

---

site_id	AC2
Number of Residues	7
Details	binding site for residue OLB A 402

Chain	Residue
A	SER196
A	ILE298
L	OLB201
A	ARG133
A	LEU153
A	CYS156
A	LEU160

---

site_id	AC3
Number of Residues	3
Details	binding site for residue OLB A 403

Chain	Residue
A	LEU214
A	SER221
A	GLN265

---

site_id	AC4
Number of Residues	8
Details	binding site for residue OLB A 404

Chain	Residue
A	MET167
A	PHE168
A	ARG169
A	PRO170
A	ASN171
A	GLN273
A	ARG331
A	OLB406

---

site_id	AC5
Number of Residues	12
Details	binding site for residue OLA A 405

Chain	Residue
A	ASP219
A	TYR220
A	ILE223
A	ARG278
A	ALA279
A	LEU320
A	TYR321
A	ALA325
A	TYR328
A	PHE351
A	HIS362
A	HOH501

---

site_id	AC6
Number of Residues	5
Details	binding site for residue OLB A 406

Chain	Residue
A	MET167
A	ASN171
A	LEU178
A	LEU186
A	OLB404

---

site_id	AC7
Number of Residues	11
Details	binding site for residue OLB L 201

Chain	Residue
A	SER131
A	PHE132
A	ARG133
A	PHE302
A	LEU303
A	OLB402
L	ASN28
L	HIS30
L	ASN31
L	GLY68
L	HOH301

---

site_id	AC8
Number of Residues	6
Details	binding site for residue GOL L 202

Chain	Residue
L	GLN37
L	LYS39
L	GLN45
L	PRO59
L	ASP82
L	HOH302

---

Functional Information from PROSITE/UniProt

site_id	PS00213
Number of Residues	12
Details	LIPOCALIN Lipocalin signature. GGS..EFEGRWRVI

Chain	Residue	Details
A	GLY-4-ILE106

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	20
Details	TRANSMEM: Helical; Name=1 => ECO:0000269|PubMed:25855295

Chain	Residue	Details
A	ASN148-PHE168

---

site_id	SWS_FT_FI2
Number of Residues	52
Details	TOPO_DOM: Extracellular => ECO:0000269|PubMed:25855295

Chain	Residue	Details
A	ARG169-LYS181
A	LEU235-PRO245
A	HIS295-GLY309
A	GLN370-LEU386

---

site_id	SWS_FT_FI3
Number of Residues	20
Details	TRANSMEM: Helical; Name=2 => ECO:0000269|PubMed:25855295

Chain	Residue	Details
A	VAL182-HIS202

---

site_id	SWS_FT_FI4
Number of Residues	33
Details	TOPO_DOM: Cytoplasmic => ECO:0000269|PubMed:25855295

Chain	Residue	Details
A	THR203-ARG213
A	ASP267-GLN273
A	ARG331-HIS348

---

site_id	SWS_FT_FI5
Number of Residues	20
Details	TRANSMEM: Helical; Name=3 => ECO:0000269|PubMed:25855295

Chain	Residue	Details
A	LEU214-TRP234

---

site_id	SWS_FT_FI6
Number of Residues	20
Details	TRANSMEM: Helical; Name=4 => ECO:0000269|PubMed:25855295

Chain	Residue	Details
A	CYS246-TRP266

---

site_id	SWS_FT_FI7
Number of Residues	20
Details	TRANSMEM: Helical; Name=5 => ECO:0000269|PubMed:25855295

Chain	Residue	Details
A	TYR274-LEU294

---

site_id	SWS_FT_FI8
Number of Residues	20
Details	TRANSMEM: Helical; Name=6 => ECO:0000269|PubMed:25855295

Chain	Residue	Details
A	GLN310-ALA330

---

site_id	SWS_FT_FI9
Number of Residues	20
Details	TRANSMEM: Helical; Name=7 => ECO:0000269|PubMed:25855295

Chain	Residue	Details
A	GLN349-LEU369

---

site_id	SWS_FT_FI10
Number of Residues	3
Details	BINDING: BINDING => ECO:0000269|PubMed:25855295

Chain	Residue	Details
A	HIS202
A	HIS348
A	HIS352

---