6YX9

Cryogenic human adiponectin receptor 2 (ADIPOR2) at 2.4 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	4
Details	binding site for residue ZN A 401

Chain	Residue
A	HIS202
A	HIS348
A	HIS352
A	OLA407

---

site_id	AC2
Number of Residues	14
Details	binding site for residue OLB A 402

Chain	Residue
A	VAL297
A	ILE298
A	PHE302
A	LEU303
A	HOH501
L	ASN28
L	HIS30
L	ASN31
L	GLY68
A	SER131
A	PHE132
A	ARG133
A	PHE136
A	LEU200

---

site_id	AC3
Number of Residues	6
Details	binding site for residue OLB A 403

Chain	Residue
A	LEU154
A	PHE158
A	CYS161
A	PHE165
A	PHE168
A	ARG169

---

site_id	AC4
Number of Residues	6
Details	binding site for residue OLB A 404

Chain	Residue
A	LEU214
A	LYS217
A	LEU218
A	SER221
A	LEU225
A	GLN265

---

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

Chain	Residue
A	MET167
A	PHE168
A	ARG169
A	ASN171
A	PRO272
A	GLN273
A	ARG275
A	ILE322
A	ALA329
A	ARG331
A	ARG335
A	HOH506

---

site_id	AC6
Number of Residues	10
Details	binding site for residue OLB A 406

Chain	Residue
A	SER230
A	GLY286
A	ILE290
A	PHE302
A	ILE311
A	LEU314
A	MET317
A	TYR321
A	HIS362
A	OLA407

---

site_id	AC7
Number of Residues	13
Details	binding site for residue OLA A 407

Chain	Residue
A	ASP219
A	ILE223
A	PHE282
A	LEU320
A	TYR321
A	TYR328
A	HIS348
A	PHE351
A	PHE354
A	GLY358
A	ZN401
A	OLB406
A	HOH502

---

site_id	AC8
Number of Residues	4
Details	binding site for residue GOL L 201

Chain	Residue
L	GLN37
L	GLN45
L	PHE62
L	ASP82

---

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	Transmembrane: {"description":"Helical; Name=1","evidences":[{"source":"PubMed","id":"25855295","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	36
Details	Topological domain: {"description":"Extracellular","evidences":[{"source":"PubMed","id":"25855295","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	20
Details	Transmembrane: {"description":"Helical; Name=2","evidences":[{"source":"PubMed","id":"25855295","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	33
Details	Topological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"25855295","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	20
Details	Transmembrane: {"description":"Helical; Name=3","evidences":[{"source":"PubMed","id":"25855295","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	20
Details	Transmembrane: {"description":"Helical; Name=4","evidences":[{"source":"PubMed","id":"25855295","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	20
Details	Transmembrane: {"description":"Helical; Name=5","evidences":[{"source":"PubMed","id":"25855295","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI8
Number of Residues	20
Details	Transmembrane: {"description":"Helical; Name=6","evidences":[{"source":"PubMed","id":"25855295","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI9
Number of Residues	20
Details	Transmembrane: {"description":"Helical; Name=7","evidences":[{"source":"PubMed","id":"25855295","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI10
Number of Residues	3
Details	Binding site: {"evidences":[{"source":"PubMed","id":"25855295","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---