6KS1

Crystal structure of the human adiponectin receptor 2

Replaces:  3WXW

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	HIS202
A	HIS348
A	HIS352
A	HOH501
A	HOH522

---

site_id	AC2
Number of Residues	12
Details	binding site for residue OLA A 402

Chain	Residue
A	LEU320
A	TYR321
A	TYR328
A	PHE351
A	PHE354
A	GLY358
A	ALA359
A	HOH522
A	TYR220
A	ARG278
A	ALA279
A	MET317

---

site_id	AC3
Number of Residues	6
Details	binding site for residue OLB A 404

Chain	Residue
A	LEU189
A	LEU193
A	LYS217
A	LEU218
A	GLN265
A	OLB406

---

site_id	AC4
Number of Residues	3
Details	binding site for residue OLB A 405

Chain	Residue
A	LEU193
A	LEU214
A	OLC408

---

site_id	AC5
Number of Residues	3
Details	binding site for residue OLB A 406

Chain	Residue
A	ILE262
A	GLN265
A	OLB404

---

site_id	AC6
Number of Residues	7
Details	binding site for residue OLB A 407

Chain	Residue
A	MET167
A	PHE168
A	LEU283
A	LEU287
A	ILE322
A	ALA326
A	OLB403

---

site_id	AC7
Number of Residues	4
Details	binding site for residue OLC A 408

Chain	Residue
A	PHE197
A	LEU200
A	PHE215
A	OLB405

---

site_id	AC8
Number of Residues	16
Details	binding site for residues OLB A 403 and LPX A 409

Chain	Residue
A	SER131
A	PHE132
A	ARG133
A	PHE136
A	CYS156
A	LEU160
A	TRP199
A	LEU287
A	LEU294
A	VAL297
A	GLY301
A	PHE302
A	OLB407
A	HOH503
L	ASN28
L	HIS30

---

site_id	AC9
Number of Residues	16
Details	binding site for residues OLB A 403 and LPX A 409

Chain	Residue
A	SER131
A	PHE132
A	ARG133
A	PHE136
A	CYS156
A	LEU160
A	TRP199
A	LEU287
A	LEU294
A	VAL297
A	GLY301
A	PHE302
A	OLB407
A	HOH503
L	ASN28
L	HIS30

---

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

---