Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6BW6

Human GPT (DPAGT1) H129 variant in complex with tunicamycin

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003975	molecular_function	UDP-N-acetylglucosamine-dolichyl-phosphate N-acetylglucosaminephosphotransferase activity
A	0003976	molecular_function	UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity
A	0005515	molecular_function	protein binding
A	0005789	cellular_component	endoplasmic reticulum membrane
A	0005794	cellular_component	Golgi apparatus
A	0006486	biological_process	obsolete protein glycosylation
A	0006487	biological_process	protein N-linked glycosylation
A	0006488	biological_process	dolichol-linked oligosaccharide biosynthetic process
A	0016020	cellular_component	membrane
A	0016740	molecular_function	transferase activity
A	0016757	molecular_function	glycosyltransferase activity
A	0016780	molecular_function	phosphotransferase activity, for other substituted phosphate groups
A	0042802	molecular_function	identical protein binding
A	0043231	cellular_component	intracellular membrane-bounded organelle
A	0046872	molecular_function	metal ion binding
B	0003975	molecular_function	UDP-N-acetylglucosamine-dolichyl-phosphate N-acetylglucosaminephosphotransferase activity
B	0003976	molecular_function	UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity
B	0005515	molecular_function	protein binding
B	0005789	cellular_component	endoplasmic reticulum membrane
B	0005794	cellular_component	Golgi apparatus
B	0006486	biological_process	obsolete protein glycosylation
B	0006487	biological_process	protein N-linked glycosylation
B	0006488	biological_process	dolichol-linked oligosaccharide biosynthetic process
B	0016020	cellular_component	membrane
B	0016740	molecular_function	transferase activity
B	0016757	molecular_function	glycosyltransferase activity
B	0016780	molecular_function	phosphotransferase activity, for other substituted phosphate groups
B	0042802	molecular_function	identical protein binding
B	0043231	cellular_component	intracellular membrane-bounded organelle
B	0046872	molecular_function	metal ion binding
C	0003975	molecular_function	UDP-N-acetylglucosamine-dolichyl-phosphate N-acetylglucosaminephosphotransferase activity
C	0003976	molecular_function	UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity
C	0005515	molecular_function	protein binding
C	0005789	cellular_component	endoplasmic reticulum membrane
C	0005794	cellular_component	Golgi apparatus
C	0006486	biological_process	obsolete protein glycosylation
C	0006487	biological_process	protein N-linked glycosylation
C	0006488	biological_process	dolichol-linked oligosaccharide biosynthetic process
C	0016020	cellular_component	membrane
C	0016740	molecular_function	transferase activity
C	0016757	molecular_function	glycosyltransferase activity
C	0016780	molecular_function	phosphotransferase activity, for other substituted phosphate groups
C	0042802	molecular_function	identical protein binding
C	0043231	cellular_component	intracellular membrane-bounded organelle
C	0046872	molecular_function	metal ion binding
D	0003975	molecular_function	UDP-N-acetylglucosamine-dolichyl-phosphate N-acetylglucosaminephosphotransferase activity
D	0003976	molecular_function	UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity
D	0005515	molecular_function	protein binding
D	0005789	cellular_component	endoplasmic reticulum membrane
D	0005794	cellular_component	Golgi apparatus
D	0006486	biological_process	obsolete protein glycosylation
D	0006487	biological_process	protein N-linked glycosylation
D	0006488	biological_process	dolichol-linked oligosaccharide biosynthetic process
D	0016020	cellular_component	membrane
D	0016740	molecular_function	transferase activity
D	0016757	molecular_function	glycosyltransferase activity
D	0016780	molecular_function	phosphotransferase activity, for other substituted phosphate groups
D	0042802	molecular_function	identical protein binding
D	0043231	cellular_component	intracellular membrane-bounded organelle
D	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	14
Details	binding site for residue TUM A 501

Chain	Residue
A	GLN44
A	PHE249
A	ASP252
A	ARG301
A	ARG303
A	ILE304
A	LEU46
A	TRP122
A	ASN182
A	ASN185
A	ILE186
A	ALA188
A	GLY189
A	ASN191

site_id	AC2
Number of Residues	10
Details	binding site for residue PGW A 502

Chain	Residue
A	ALA31
A	PHE32
A	HIS35
A	ILE68
B	CYS107
B	PHE110
B	LEU111
B	ALA114
B	HIS124
B	LEU128

site_id	AC3
Number of Residues	11
Details	binding site for residue PGW B 501

Chain	Residue
A	CYS107
A	PHE110
A	ALA114
A	LEU118
A	HIS124
B	LEU28
B	ALA31
B	PHE32
B	HIS35
B	ILE68
B	PHE71

site_id	AC4
Number of Residues	17
Details	binding site for residue TUM B 502

Chain	Residue
B	GLN44
B	ASP45
B	LEU46
B	TRP122
B	LYS125
B	ASN185
B	ILE186
B	ALA188
B	GLY189
B	ILE190
B	ASN191
B	PHE249
B	ASP252
B	LEU293
B	HIS302
B	ARG303
B	ILE304

site_id	AC5
Number of Residues	17
Details	binding site for residue TUM C 501

Chain	Residue
C	GLN44
C	ASP45
C	LEU46
C	TRP122
C	ASN185
C	ILE186
C	ALA188
C	GLY189
C	ILE190
C	ASN191
C	PHE249
C	ASP252
C	LEU293
C	ARG301
C	HIS302
C	ARG303
C	ILE304

site_id	AC6
Number of Residues	12
Details	binding site for residue PGW C 502

Chain	Residue
C	CYS107
C	PHE110
C	ALA114
C	LEU118
C	HIS124
D	LEU28
D	ALA31
D	PHE32
D	HIS35
D	ALA64
D	ILE68
D	PHE71

site_id	AC7
Number of Residues	13
Details	binding site for residue PGW C 503

Chain	Residue
C	LEU28
C	ALA31
C	PHE32
C	HIS35
C	ILE68
C	PHE71
D	CYS107
D	PHE110
D	LEU111
D	ALA114
D	LEU118
D	HIS124
D	LEU127

site_id	AC8
Number of Residues	18
Details	binding site for residue TUM D 501

Chain	Residue
D	ASN185
D	ILE186
D	ALA188
D	GLY189
D	ILE190
D	ASN191
D	PHE249
D	ASP252
D	LEU293
D	ARG301
D	HIS302
D	ARG303
D	ILE304
D	GLN44
D	ASP45
D	LEU46
D	TRP122
D	LYS125

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	108
Details	Transmembrane: {"description":"Helical; Name=Helix 1","evidences":[{"source":"PubMed","id":"29459785","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	132
Details	Topological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"29459785","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	76
Details	Transmembrane: {"description":"Helical; Name=Helix 2","evidences":[{"source":"PubMed","id":"29459785","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	104
Details	Transmembrane: {"description":"Helical; Name=Helix 3","evidences":[{"source":"PubMed","id":"29459785","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	84
Details	Transmembrane: {"description":"Helical; Name=Helix 4","evidences":[{"source":"PubMed","id":"29459785","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	76
Details	Transmembrane: {"description":"Helical; Name=Helix 5","evidences":[{"source":"PubMed","id":"29459785","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	80
Details	Transmembrane: {"description":"Helical; Name=Helix 6","evidences":[{"source":"PubMed","id":"29459785","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	20
Details	Topological domain: {"description":"Lumenal","evidences":[{"source":"PubMed","id":"29459785","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	92
Details	Transmembrane: {"description":"Helical; Name=Helix 7","evidences":[{"source":"PubMed","id":"29459785","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	72
Details	Transmembrane: {"description":"Helical; Name=Helix 8","evidences":[{"source":"PubMed","id":"29459785","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	84
Details	Transmembrane: {"description":"Helical; Name=Helix 9","evidences":[{"source":"PubMed","id":"29459785","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI12
Number of Residues	24
Details	Binding site: {"evidences":[{"source":"PubMed","id":"30388443","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI13
Number of Residues	8
Details	Binding site: {"evidences":[{"source":"PubMed","id":"29459785","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6BW5","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6BW6","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI14
Number of Residues	8
Details	Binding site: {"evidences":[{"source":"PubMed","id":"29459785","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6BW5","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI15
Number of Residues	36
Details	Binding site: {"evidences":[{"source":"PubMed","id":"30388443","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI16
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"29459785","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6BW6","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI17
Number of Residues	4
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI18
Number of Residues	72
Details	Transmembrane: {"description":"Helical; Name=Helix 10","evidences":[{"source":"PubMed","id":"29459785","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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