6IIV

Crystal structure of the human thromboxane A2 receptor bound to daltroban

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004930	molecular_function	G protein-coupled receptor activity
A	0004960	molecular_function	thromboxane receptor activity
A	0005506	molecular_function	iron ion binding
A	0007186	biological_process	G protein-coupled receptor signaling pathway
A	0009055	molecular_function	electron transfer activity
A	0016020	cellular_component	membrane
A	0020037	molecular_function	heme binding
A	0022900	biological_process	electron transport chain
A	0042597	cellular_component	periplasmic space
A	0043448	biological_process	alkane catabolic process
A	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	15
Details	binding site for residue A90 A 9001

Chain	Residue
A	GLY77
A	TRP258
A	LEU291
A	LEU294
A	ARG295
A	THR298
A	GLN301
A	LEU78
A	THR81
A	VAL85
A	HIS89
A	MET112
A	SER181
A	TRP182
A	PHE184

---

site_id	AC2
Number of Residues	4
Details	binding site for residue ZN A 9002

Chain	Residue
A	CYS2006
A	CYS2009
A	CYS2039
A	CYS2042

---

site_id	AC3
Number of Residues	8
Details	binding site for residue CLR A 9003

Chain	Residue
A	ARG103
A	PHE107
A	VAL110
A	TRP150
A	GLY154
A	TRP157
A	LEU161
A	LEU168

---

site_id	AC4
Number of Residues	5
Details	binding site for residue GOL A 9004

Chain	Residue
A	GLU94
A	TRP95
A	HIS96
A	GLN1103
A	ASP2036

---

Functional Information from PROSITE/UniProt

site_id	PS00202
Number of Residues	11
Details	RUBREDOXIN Rubredoxin signature. IpDDWvCPlCG

Chain	Residue	Details
A	ILE2033-GLY2043

---

site_id	PS00237
Number of Residues	17
Details	G_PROTEIN_RECEP_F1_1 G-protein coupled receptors family 1 signature. SPLlLGAAMASERYLgI

Chain	Residue	Details
A	SER118-ILE134

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	BINDING: axial binding residue

Chain	Residue	Details
A	TRP1007
A	ILE1102

---

site_id	SWS_FT_FI2
Number of Residues	22
Details	TRANSMEM: Helical; Name=1 => ECO:0000255

Chain	Residue	Details
A	PHE30-ALA52

---

site_id	SWS_FT_FI3
Number of Residues	33
Details	TOPO_DOM: Cytoplasmic => ECO:0000255

Chain	Residue	Details
A	ARG53-PHE66
A	GLU129-ALA149

---

site_id	SWS_FT_FI4
Number of Residues	20
Details	TRANSMEM: Helical; Name=2 => ECO:0000255

Chain	Residue	Details
A	LEU67-SER87

---

site_id	SWS_FT_FI5
Number of Residues	56
Details	TOPO_DOM: Extracellular => ECO:0000255

Chain	Residue	Details
A	GLN88-ARG106
A	ARG173-ASP193
A	ARG271-GLU289

---

site_id	SWS_FT_FI6
Number of Residues	21
Details	TRANSMEM: Helical; Name=3 => ECO:0000255

Chain	Residue	Details
A	PHE107-SER128

---

site_id	SWS_FT_FI7
Number of Residues	22
Details	TRANSMEM: Helical; Name=4 => ECO:0000255

Chain	Residue	Details
A	TRP150-GLY172

---

site_id	SWS_FT_FI8
Number of Residues	25
Details	TRANSMEM: Helical; Name=5 => ECO:0000255

Chain	Residue	Details
A	VAL194-VAL219

---

site_id	SWS_FT_FI9
Number of Residues	23
Details	TRANSMEM: Helical; Name=6 => ECO:0000255

Chain	Residue	Details
A	ALA247-LEU270

---

site_id	SWS_FT_FI10
Number of Residues	21
Details	TRANSMEM: Helical; Name=7 => ECO:0000255

Chain	Residue	Details
A	LEU290-PHE311

---

site_id	SWS_FT_FI11
Number of Residues	1
Details	CARBOHYD: N-linked (GlcNAc...) asparagine

Chain	Residue	Details
A	ASN16

---

site_id	SWS_FT_FI12
Number of Residues	4
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00241, ECO:0000269|PubMed:10216292

Chain	Residue	Details
A	CYS2006
A	CYS2009
A	CYS2039
A	CYS2042

---

site_id	SWS_FT_FI13
Number of Residues	1
Details	MOD_RES: N-formylmethionine => ECO:0000269|PubMed:1637309

Chain	Residue	Details
A	MET2001

---