Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4ZW9

Crystal structure of human GLUT3 bound to D-glucose in the outward-occluded conformation at 1.5 angstrom

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 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	146
Details	TOPO_DOM: Cytoplasmic => ECO:0000305

Chain	Residue	Details
A	MET1-LEU10
A	ASN86-ARG90
A	GLY143-ALA153
A	CYS205-PRO269
A	VAL326-ARG331
A	ALA390-PRO399
A	PRO451-VAL496

site_id	SWS_FT_FI2
Number of Residues	21
Details	TRANSMEM: Helical; Name=1 => ECO:0000255, ECO:0000269\|PubMed:26176916

Chain	Residue	Details
A	ILE11-ASN32

site_id	SWS_FT_FI3
Number of Residues	76
Details	TOPO_DOM: Extracellular => ECO:0000305

Chain	Residue	Details
A	ALA33-SER64
A	LYS112-GLU118
A	GLU175-LEU183
A	TYR291-PRO304
A	LEU353-SER363
A	PRO421-ALA429

site_id	SWS_FT_FI4
Number of Residues	20
Details	TRANSMEM: Helical; Name=2 => ECO:0000255, ECO:0000269\|PubMed:26176916

Chain	Residue	Details
A	LEU65-VAL85

site_id	SWS_FT_FI5
Number of Residues	20
Details	TRANSMEM: Helical; Name=3 => ECO:0000255, ECO:0000269\|PubMed:26176916

Chain	Residue	Details
A	ARG91-CYS111

site_id	SWS_FT_FI6
Number of Residues	23
Details	TRANSMEM: Helical; Name=4 => ECO:0000255, ECO:0000269\|PubMed:26176916

Chain	Residue	Details
A	MET119-ILE142

site_id	SWS_FT_FI7
Number of Residues	20
Details	TRANSMEM: Helical; Name=5 => ECO:0000255, ECO:0000269\|PubMed:26176916

Chain	Residue	Details
A	PHE154-LEU174

site_id	SWS_FT_FI8
Number of Residues	20
Details	TRANSMEM: Helical; Name=6 => ECO:0000255, ECO:0000269\|PubMed:26176916

Chain	Residue	Details
A	TRP184-PHE204

site_id	SWS_FT_FI9
Number of Residues	20
Details	TRANSMEM: Helical; Name=7 => ECO:0000255, ECO:0000269\|PubMed:26176916

Chain	Residue	Details
A	ILE270-TYR290

site_id	SWS_FT_FI10
Number of Residues	20
Details	TRANSMEM: Helical; Name=8 => ECO:0000255, ECO:0000269\|PubMed:26176916

Chain	Residue	Details
A	ILE305-LEU325

site_id	SWS_FT_FI11
Number of Residues	20
Details	TRANSMEM: Helical; Name=9 => ECO:0000255, ECO:0000269\|PubMed:26176916

Chain	Residue	Details
A	ARG332-SER352

site_id	SWS_FT_FI12
Number of Residues	25
Details	TRANSMEM: Helical; Name=10 => ECO:0000255, ECO:0000269\|PubMed:26176916

Chain	Residue	Details
A	PHE364-VAL389

site_id	SWS_FT_FI13
Number of Residues	20
Details	TRANSMEM: Helical; Name=11 => ECO:0000255, ECO:0000269\|PubMed:26176916

Chain	Residue	Details
A	ALA400-PHE420

site_id	SWS_FT_FI14
Number of Residues	20
Details	TRANSMEM: Helical; Name=12 => ECO:0000255, ECO:0000269\|PubMed:26176916

Chain	Residue	Details
A	TYR430-VAL450

site_id	SWS_FT_FI15
Number of Residues	6
Details	BINDING: BINDING => ECO:0000269\|PubMed:26176916, ECO:0007744\|PDB:4ZW9

Chain	Residue	Details
A	GLN159
A	GLN280
A	ASN286
A	ASN315
A	GLU378
A	TRP386

site_id	SWS_FT_FI16
Number of Residues	1
Details	MOD_RES: Phosphothreonine => ECO:0000250\|UniProtKB:P32037

Chain	Residue	Details
A	THR232

site_id	SWS_FT_FI17
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0000250\|UniProtKB:P32037

Chain	Residue	Details
A	SER475

site_id	SWS_FT_FI18
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0000250\|UniProtKB:Q07647

Chain	Residue	Details
A	SER485

site_id	SWS_FT_FI19
Number of Residues	1
Details	MOD_RES: Phosphothreonine => ECO:0000250\|UniProtKB:Q07647

Chain	Residue	Details
A	THR492

site_id	SWS_FT_FI20
Number of Residues	1
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255

Chain	Residue	Details
A	THR43

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)