3HFX

Crystal structure of carnitine transporter

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005886	cellular_component	plasma membrane
A	0009437	biological_process	carnitine metabolic process
A	0015226	molecular_function	carnitine transmembrane transporter activity
A	0015297	molecular_function	antiporter activity
A	0015879	biological_process	carnitine transport
A	0016020	cellular_component	membrane
A	0022857	molecular_function	transmembrane transporter activity
A	0044667	molecular_function	(R)-carnitine:4-(trimethylammonio)butanoate antiporter activity
A	0071705	biological_process	nitrogen compound transport
A	1900749	biological_process	(R)-carnitine transport
A	1900751	biological_process	4-(trimethylammonio)butanoate transport
A	1902270	biological_process	(R)-carnitine transmembrane transport
A	1902603	biological_process	carnitine transmembrane transport

Functional Information from PDB Data

site_id	AC1
Number of Residues	1
Details	BINDING SITE FOR RESIDUE HG A 505

Chain	Residue
A	CYS481

---

site_id	AC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE HG A 506

Chain	Residue
A	CYS99
A	THR100
A	SER101

---

site_id	AC3
Number of Residues	2
Details	BINDING SITE FOR RESIDUE HG A 507

Chain	Residue
A	CYS238
A	LEU242

---

site_id	AC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE HG A 508

Chain	Residue
A	CYS26
A	ILE459
A	VAL462

---

site_id	AC5
Number of Residues	3
Details	BINDING SITE FOR RESIDUE HG A 509

Chain	Residue
A	MET204
A	LEU422
A	CYS426

---

site_id	AC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE HG A 510

Chain	Residue
A	LEU214
A	VAL215
A	CYS218
A	PHE411
A	PHE412
A	CYS415

---

site_id	AC7
Number of Residues	3
Details	BINDING SITE FOR RESIDUE HG A 511

Chain	Residue
A	MET204
A	CYS426
A	152602

---

site_id	AC8
Number of Residues	3
Details	BINDING SITE FOR RESIDUE HG A 512

Chain	Residue
A	LEU251
A	GLN252
A	VAL255

---

site_id	AC9
Number of Residues	2
Details	BINDING SITE FOR RESIDUE HG A 513

Chain	Residue
A	ALA248
A	CYS249

---

site_id	BC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE 152 A 601

Chain	Residue
A	SER101
A	VAL104
A	TRP323
A	TRP324
A	TYR327

---

site_id	BC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE 152 A 602

Chain	Residue
A	TYR327
A	GLN330
A	MET331
A	PHE334
A	LEU422
A	HG511

---

site_id	BC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE 152 A 603

Chain	Residue
A	TYR114
A	GLY310
A	GLY311
A	TRP316

---

site_id	BC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE 152 A 604

Chain	Residue
A	GLU85
A	PHE86
A	ARG337
A	ILE338

---

Functional Information from PROSITE/UniProt

site_id	PS01303
Number of Residues	10
Details	BCCT BCCT family of transporters signature. GWTVfYWaWW

Chain	Residue	Details
A	GLY315-TRP324

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	111
Details	TOPO_DOM: Cytoplasmic => ECO:0000269|PubMed:20357772, ECO:0007744|PDB:3HFX

Chain	Residue	Details
A	MET1-PRO12
A	TRP68-SER90
A	PHE152-GLY186
A	CYS249-LYS253
A	ALA336-PHE349
A	MET432-LEU446
A	THR491-ASP504

---

site_id	SWS_FT_FI2
Number of Residues	242
Details	TRANSMEM: Helical => ECO:0000269|PubMed:20357772, ECO:0007744|PDB:3HFX

Chain	Residue	Details
A	LYS13-VAL30
A	SER404-ALA431
A	LEU447-LEU466
A	LEU469-VAL490
A	GLY52-PHE67
A	TRP91-SER98
A	GLU132-SER151
A	LEU187-MET219
A	LEU231-ALA248
A	GLY254-SER277
A	PHE312-LEU335
A	GLY350-LEU372

---

site_id	SWS_FT_FI3
Number of Residues	126
Details	TOPO_DOM: Periplasmic => ECO:0000269|PubMed:20357772, ECO:0007744|PDB:3HFX

Chain	Residue	Details
A	ARG31-TRP51
A	CYS99-LYS131
A	GLN220-GLN230
A	GLY278-GLY311
A	LEU373-LEU403
A	GLY467-GLY468

---

site_id	SWS_FT_FI4
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269|PubMed:20829798, ECO:0007744|PDB:2WSX

Chain	Residue	Details
A	TYR114
A	GLY315
A	TRP323
A	MET331

---

site_id	SWS_FT_FI5
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269|PubMed:20357772, ECO:0007744|PDB:3HFX

Chain	Residue	Details
A	TRP142
A	TYR327

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