4JKV

Structure of the human smoothened 7TM receptor in complex with an antitumor agent

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004888	molecular_function	transmembrane signaling receptor activity
A	0005506	molecular_function	iron ion binding
A	0007166	biological_process	cell surface 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	0046872	molecular_function	metal ion binding
B	0004888	molecular_function	transmembrane signaling receptor activity
B	0005506	molecular_function	iron ion binding
B	0007166	biological_process	cell surface receptor signaling pathway
B	0009055	molecular_function	electron transfer activity
B	0016020	cellular_component	membrane
B	0020037	molecular_function	heme binding
B	0022900	biological_process	electron transport chain
B	0042597	cellular_component	periplasmic space
B	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	17
Details	BINDING SITE FOR RESIDUE 1KS A 601

Chain	Residue
A	ASN219
A	ARG400
A	GLN477
A	TRP480
A	GLU481
A	PRO513
A	GLU518
A	ASN521
A	LEU522
A	LEU221
A	TRP281
A	ASP384
A	VAL386
A	SER387
A	PHE391
A	TYR394
A	LYS395

---

site_id	AC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE OLC A 602

Chain	Residue
A	GLU447
A	ARG451
A	THR534

---

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE OLC A 603

Chain	Residue
A	TYR397
A	ARG398
A	ALA401
A	ALA406
A	PHE474
B	ALA377

---

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE OLC A 604

Chain	Residue
A	SER468
A	TYR472
A	PHE475
A	ASN476

---

site_id	AC5
Number of Residues	2
Details	BINDING SITE FOR RESIDUE OLA A 605

Chain	Residue
A	GLY288
A	ILE316

---

site_id	AC6
Number of Residues	3
Details	BINDING SITE FOR RESIDUE OLA A 606

Chain	Residue
A	TYR323
A	HIS361
A	TRP365

---

site_id	AC7
Number of Residues	2
Details	BINDING SITE FOR RESIDUE PEG A 607

Chain	Residue
A	PRO220
A	LEU221

---

site_id	AC8
Number of Residues	6
Details	BINDING SITE FOR RESIDUE PGE A 608

Chain	Residue
A	GLN380
A	ASN396
A	TYR399
A	HOH714
B	ASN396
B	TYR399

---

site_id	AC9
Number of Residues	3
Details	BINDING SITE FOR RESIDUE PG4 A 609

Chain	Residue
A	ASP229
A	TYR233
A	LYS519

---

site_id	BC1
Number of Residues	19
Details	BINDING SITE FOR RESIDUE 1KS B 601

Chain	Residue
B	ASN219
B	LEU221
B	MET230
B	TRP281
B	MET301
B	ASP384
B	VAL386
B	SER387
B	PHE391
B	TYR394
B	LYS395
B	ARG400
B	GLN477
B	TRP480
B	GLU481
B	PRO513
B	GLU518
B	ASN521
B	LEU522

---

site_id	BC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE OLC B 602

Chain	Residue
B	ASP287
B	GLU292
B	ILE293

---

site_id	BC3
Number of Residues	2
Details	BINDING SITE FOR RESIDUE OLC B 603

Chain	Residue
B	TYR233
B	LYS519

---

site_id	BC4
Number of Residues	2
Details	BINDING SITE FOR RESIDUE OLA B 604

Chain	Residue
B	ILE413
B	TYR417

---

site_id	BC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PEG B 605

Chain	Residue
B	THR311
B	LEU312
B	SER313
B	HOH759

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	44
Details	Region: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	26
Details	Compositional bias: {"description":"Basic and acidic residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	4
Details	Binding site: {"description":"axial binding residue"}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	40
Details	Transmembrane: {"description":"Helical; Name=1","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	68
Details	Topological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	40
Details	Transmembrane: {"description":"Helical; Name=2","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	104
Details	Topological domain: {"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI8
Number of Residues	40
Details	Transmembrane: {"description":"Helical; Name=3","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI9
Number of Residues	40
Details	Transmembrane: {"description":"Helical; Name=4","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI10
Number of Residues	40
Details	Transmembrane: {"description":"Helical; Name=5","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI11
Number of Residues	40
Details	Transmembrane: {"description":"Helical; Name=6","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI12
Number of Residues	40
Details	Transmembrane: {"description":"Helical; Name=7","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI13
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P56726","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI14
Number of Residues	2
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---