Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1GUQ

STRUCTURE OF NUCLEOTIDYLTRANSFERASE COMPLEXED WITH UDP-GLUCOSE

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004335	molecular_function	galactokinase activity
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006012	biological_process	galactose metabolic process
A	0008108	molecular_function	UDP-glucose:hexose-1-phosphate uridylyltransferase activity
A	0008198	molecular_function	ferrous iron binding
A	0008270	molecular_function	zinc ion binding
A	0016740	molecular_function	transferase activity
A	0016779	molecular_function	nucleotidyltransferase activity
A	0033499	biological_process	galactose catabolic process via UDP-galactose, Leloir pathway
A	0046835	biological_process	carbohydrate phosphorylation
A	0046872	molecular_function	metal ion binding
B	0004335	molecular_function	galactokinase activity
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0006012	biological_process	galactose metabolic process
B	0008108	molecular_function	UDP-glucose:hexose-1-phosphate uridylyltransferase activity
B	0008198	molecular_function	ferrous iron binding
B	0008270	molecular_function	zinc ion binding
B	0016740	molecular_function	transferase activity
B	0016779	molecular_function	nucleotidyltransferase activity
B	0033499	biological_process	galactose catabolic process via UDP-galactose, Leloir pathway
B	0046835	biological_process	carbohydrate phosphorylation
B	0046872	molecular_function	metal ion binding
C	0004335	molecular_function	galactokinase activity
C	0005737	cellular_component	cytoplasm
C	0005829	cellular_component	cytosol
C	0006012	biological_process	galactose metabolic process
C	0008108	molecular_function	UDP-glucose:hexose-1-phosphate uridylyltransferase activity
C	0008198	molecular_function	ferrous iron binding
C	0008270	molecular_function	zinc ion binding
C	0016740	molecular_function	transferase activity
C	0016779	molecular_function	nucleotidyltransferase activity
C	0033499	biological_process	galactose catabolic process via UDP-galactose, Leloir pathway
C	0046835	biological_process	carbohydrate phosphorylation
C	0046872	molecular_function	metal ion binding
D	0004335	molecular_function	galactokinase activity
D	0005737	cellular_component	cytoplasm
D	0005829	cellular_component	cytosol
D	0006012	biological_process	galactose metabolic process
D	0008108	molecular_function	UDP-glucose:hexose-1-phosphate uridylyltransferase activity
D	0008198	molecular_function	ferrous iron binding
D	0008270	molecular_function	zinc ion binding
D	0016740	molecular_function	transferase activity
D	0016779	molecular_function	nucleotidyltransferase activity
D	0033499	biological_process	galactose catabolic process via UDP-galactose, Leloir pathway
D	0046835	biological_process	carbohydrate phosphorylation
D	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN A 350

Chain	Residue
A	CYS52
A	CYS55
A	HIS115
A	HIS164

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE FE A 351

Chain	Residue
A	GLU182
A	HIS281
A	HIS296
A	HIS298

site_id	AC3
Number of Residues	7
Details	BINDING SITE FOR RESIDUE K A 353

Chain	Residue
A	GLY166
A	HOH354
A	HOH382
A	HOH394
A	HOH492
A	HOH503
A	ASN153

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN B 350

Chain	Residue
B	CYS52
B	CYS55
B	HIS115
B	HIS164

site_id	AC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE FE B 351

Chain	Residue
B	GLU182
B	HIS281
B	HIS296
B	HIS298

site_id	AC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE K B 353

Chain	Residue
B	ASN153
B	GLY166
B	HOH360
B	HOH372
B	HOH427
B	HOH479

site_id	AC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN C 350

Chain	Residue
C	CYS52
C	CYS55
C	HIS115
C	HIS164

site_id	AC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE FE C 351

Chain	Residue
C	LEU17
C	GLU182
C	HIS281
C	HIS296
C	HIS298

site_id	AC9
Number of Residues	6
Details	BINDING SITE FOR RESIDUE K C 353

Chain	Residue
C	ASN153
C	GLY166
C	HOH877
C	HOH899
C	HOH925
C	HOH957

site_id	BC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN D 350

Chain	Residue
D	CYS52
D	CYS55
D	HIS115
D	HIS164

site_id	BC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE FE D 351

Chain	Residue
D	GLU182
D	HIS281
D	HIS296
D	HIS298

site_id	BC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE K D 353

Chain	Residue
D	ASN153
D	GLY166
D	HOH743
D	HOH750
D	HOH955
D	HOH1050

site_id	BC4
Number of Residues	25
Details	BINDING SITE FOR RESIDUE UPG A 352

Chain	Residue
A	PHE53
A	ARG60
A	VAL61
A	PHE75
A	ASN77
A	ASP78
A	ASN153
A	GLY159
A	CYS160
A	SER161
A	GLN168
A	HOH354
A	HOH357
A	HOH492
B	ARG28
B	ARG31
B	TRP33
B	LYS311
B	PHE312
B	VAL314
B	GLY315
B	TYR316
B	GLU317
B	GLN323
B	HOH438

site_id	BC5
Number of Residues	25
Details	BINDING SITE FOR RESIDUE UPG B 352

Chain	Residue
B	ASP78
B	ASN153
B	GLY159
B	CYS160
B	SER161
B	GLN168
B	HOH355
B	HOH413
B	HOH427
A	ARG28
A	ARG31
A	TRP33
A	LYS311
A	PHE312
A	VAL314
A	GLY315
A	TYR316
A	GLU317
A	GLN323
A	HOH526
B	PHE53
B	ARG60
B	VAL61
B	PHE75
B	ASN77

site_id	BC6
Number of Residues	25
Details	BINDING SITE FOR RESIDUE UPG C 352

Chain	Residue
C	PHE53
C	VAL61
C	PHE75
C	ASN77
C	ASP78
C	ASN153
C	GLY159
C	CYS160
C	SER161
C	GLN168
C	TRP170
C	HOH755
C	HOH812
C	HOH899
C	HOH957
D	ARG28
D	ARG31
D	TRP33
D	LYS311
D	PHE312
D	VAL314
D	GLY315
D	TYR316
D	GLU317
D	GLN323

site_id	BC7
Number of Residues	27
Details	BINDING SITE FOR RESIDUE UPG D 352

Chain	Residue
C	ARG28
C	ARG31
C	TRP33
C	LYS311
C	PHE312
C	VAL314
C	GLY315
C	TYR316
C	GLU317
C	GLN323
C	HOH777
C	HOH811
D	PHE53
D	ARG60
D	VAL61
D	PHE75
D	ASN77
D	ASP78
D	PHE79
D	PHE151
D	ASN153
D	GLY159
D	CYS160
D	SER161
D	GLN168
D	HOH836
D	HOH1050

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	Active site: {"description":"Tele-UMP-histidine intermediate","evidences":[{"source":"PROSITE-ProRule","id":"PRU10033","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"8794735","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9063869","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	20
Details	Binding site: {"evidences":[{"source":"PubMed","id":"9063869","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1GUQ","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	32
Details	Binding site: {"evidences":[{"source":"PubMed","id":"8794735","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9063869","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1GUQ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1HXQ","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	28
Details	Binding site: {"description":"in other chain","evidences":[{"source":"PubMed","id":"9063869","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1GUQ","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	CSA1
Number of Residues	4
Details	Annotated By Reference To The Literature 1hxq

Chain	Residue	Details
A	HIS164
A	GLY166
A	CYS160
A	GLN168

site_id	CSA2
Number of Residues	4
Details	Annotated By Reference To The Literature 1hxq

Chain	Residue	Details
B	HIS164
B	GLY166
B	CYS160
B	GLN168

site_id	CSA3
Number of Residues	4
Details	Annotated By Reference To The Literature 1hxq

Chain	Residue	Details
C	HIS164
C	GLY166
C	CYS160
C	GLN168

site_id	CSA4
Number of Residues	4
Details	Annotated By Reference To The Literature 1hxq

Chain	Residue	Details
D	HIS164
D	GLY166
D	CYS160
D	GLN168

site_id	MCSA1
Number of Residues	8
Details	M-CSA 88

Chain	Residue	Details
A	CYS52	metal ligand
A	CYS55	metal ligand
A	HIS115	metal ligand
A	ASN153	activator, hydrogen bond donor
A	SER161	electrostatic stabiliser, hydrogen bond donor, steric role
A	HIS164	activator
A	GLY166	hydrogen bond donor, nucleofuge, nucleophile
A	GLN168	electrostatic stabiliser, hydrogen bond donor

site_id	MCSA2
Number of Residues	8
Details	M-CSA 88

Chain	Residue	Details
B	CYS52	metal ligand
B	CYS55	metal ligand
B	HIS115	metal ligand
B	ASN153	activator, hydrogen bond donor
B	SER161	electrostatic stabiliser, hydrogen bond donor, steric role
B	HIS164	activator
B	GLY166	hydrogen bond donor, nucleofuge, nucleophile
B	GLN168	electrostatic stabiliser, hydrogen bond donor

site_id	MCSA3
Number of Residues	8
Details	M-CSA 88

Chain	Residue	Details
C	CYS52	metal ligand
C	CYS55	metal ligand
C	HIS115	metal ligand
C	ASN153	activator, hydrogen bond donor
C	SER161	electrostatic stabiliser, hydrogen bond donor, steric role
C	HIS164	activator
C	GLY166	hydrogen bond donor, nucleofuge, nucleophile
C	GLN168	electrostatic stabiliser, hydrogen bond donor

site_id	MCSA4
Number of Residues	8
Details	M-CSA 88

Chain	Residue	Details
D	CYS52	metal ligand
D	CYS55	metal ligand
D	HIS115	metal ligand
D	ASN153	activator, hydrogen bond donor
D	SER161	electrostatic stabiliser, hydrogen bond donor, steric role
D	HIS164	activator
D	GLY166	hydrogen bond donor, nucleofuge, nucleophile
D	GLN168	electrostatic stabiliser, hydrogen bond donor

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)