7CRZ

Crystal structure of human glucose transporter GLUT3 bound with C3361

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005353	molecular_function	fructose transmembrane transporter activity
A	0005354	molecular_function	galactose transmembrane transporter activity
A	0005515	molecular_function	protein binding
A	0005536	molecular_function	D-glucose binding
A	0005886	cellular_component	plasma membrane
A	0005975	biological_process	carbohydrate metabolic process
A	0015755	biological_process	fructose transmembrane transport
A	0015757	biological_process	galactose transmembrane transport
A	0016020	cellular_component	membrane
A	0016235	cellular_component	aggresome
A	0019852	biological_process	L-ascorbic acid metabolic process
A	0022857	molecular_function	transmembrane transporter activity
A	0030667	cellular_component	secretory granule membrane
A	0033300	molecular_function	dehydroascorbic acid transmembrane transporter activity
A	0035579	cellular_component	specific granule membrane
A	0042995	cellular_component	cell projection
A	0043204	cellular_component	perikaryon
A	0046323	biological_process	D-glucose import
A	0055056	molecular_function	D-glucose transmembrane transporter activity
A	0055085	biological_process	transmembrane transport
A	0070062	cellular_component	extracellular exosome
A	0070821	cellular_component	tertiary granule membrane
A	0070837	biological_process	dehydroascorbic acid transport
A	0098708	biological_process	D-glucose import across plasma membrane
A	0101003	cellular_component	ficolin-1-rich granule membrane
A	0150104	biological_process	transport across blood-brain barrier
A	1904659	biological_process	D-glucose transmembrane transport

Functional Information from PDB Data

site_id	AC1
Number of Residues	19
Details	binding site for residue F00 A 500

Chain	Residue
A	PHE24
A	GLN281
A	ASN286
A	ASN315
A	PHE377
A	GLU378
A	TRP386
A	ASN413
A	PHE414
A	GLY417
A	OLC501
A	THR28
A	ALA68
A	SER71
A	GLN159
A	ILE162
A	VAL163
A	ILE166
A	GLN280

---

site_id	AC2
Number of Residues	8
Details	binding site for residue OLC A 501

Chain	Residue
A	GLY29
A	ASN32
A	ASN286
A	PHE289
A	TYR290
A	THR293
A	F00500
A	HOH626

---

site_id	AC3
Number of Residues	7
Details	binding site for residue OLC A 502

Chain	Residue
A	THR18
A	PHE22
A	LEU157
A	LEU160
A	GLY161
A	PRO194
A	OLC505

---

site_id	AC4
Number of Residues	10
Details	binding site for residue OLC A 503

Chain	Residue
A	PHE204
A	ARG332
A	THR333
A	MET336
A	ILE337
A	GLY340
A	GLY341
A	PHE344
A	GLU452
A	ARG454

---

site_id	AC5
Number of Residues	6
Details	binding site for residue OLC A 504

Chain	Residue
A	CYS106
A	VAL113
A	TYR426
A	LEU427
A	GLY437
A	THR441

---

site_id	AC6
Number of Residues	8
Details	binding site for residue OLC A 505

Chain	Residue
A	ILE196
A	LEU197
A	ALA200
A	PHE344
A	THR347
A	TYR359
A	GLY361
A	OLC502

---

site_id	AC7
Number of Residues	4
Details	binding site for residue OLC A 506

Chain	Residue
A	PHE318
A	ILE337
A	PHE376
A	ILE379

---

Functional Information from PROSITE/UniProt

site_id	PS00216
Number of Residues	17
Details	SUGAR_TRANSPORT_1 Sugar transport proteins signature 1. SLFLVERAGRRtlhmi.G

Chain	Residue	Details
A	SER322-GLY338

---

site_id	PS00217
Number of Residues	26
Details	SUGAR_TRANSPORT_2 Sugar transport proteins signature 2. ViGLFcGLctgfvpmYigEisptalR

Chain	Residue	Details
A	VAL126-ARG151

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	21
Details	Transmembrane: {"description":"Helical; Name=1","evidences":[{"evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"26176916","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	76
Details	Topological domain: {"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	20
Details	Transmembrane: {"description":"Helical; Name=2","evidences":[{"evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"26176916","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	92
Details	Topological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	20
Details	Transmembrane: {"description":"Helical; Name=3","evidences":[{"evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"26176916","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	23
Details	Transmembrane: {"description":"Helical; Name=4","evidences":[{"evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"26176916","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	20
Details	Transmembrane: {"description":"Helical; Name=5","evidences":[{"evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"26176916","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI8
Number of Residues	20
Details	Transmembrane: {"description":"Helical; Name=6","evidences":[{"evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"26176916","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI9
Number of Residues	20
Details	Transmembrane: {"description":"Helical; Name=7","evidences":[{"evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"26176916","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI10
Number of Residues	20
Details	Transmembrane: {"description":"Helical; Name=8","evidences":[{"evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"26176916","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI11
Number of Residues	20
Details	Transmembrane: {"description":"Helical; Name=9","evidences":[{"evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"26176916","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI12
Number of Residues	25
Details	Transmembrane: {"description":"Helical; Name=10","evidences":[{"evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"26176916","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI13
Number of Residues	20
Details	Transmembrane: {"description":"Helical; Name=11","evidences":[{"evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"26176916","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI14
Number of Residues	20
Details	Transmembrane: {"description":"Helical; Name=12","evidences":[{"evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"26176916","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI15
Number of Residues	2
Details	Region: {"description":"Important for selectivity against fructose","evidences":[{"source":"PubMed","id":"26176916","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI16
Number of Residues	6
Details	Binding site: {"evidences":[{"source":"PubMed","id":"26176916","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4ZW9","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI17
Number of Residues	1
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P32037","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI18
Number of Residues	1
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---