Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2WTX

Insight into the mechanism of enzymatic glycosyltransfer with retention through the synthesis and analysis of bisubstrate glycomimetics of trehalose-6-phosphate synthase

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0003825	molecular_function	alpha,alpha-trehalose-phosphate synthase (UDP-forming) activity
A	0005992	biological_process	trehalose biosynthetic process
A	0006950	biological_process	response to stress
A	0006970	biological_process	response to osmotic stress
A	0006974	biological_process	DNA damage response
A	0016740	molecular_function	transferase activity
A	0016757	molecular_function	glycosyltransferase activity
A	0016758	molecular_function	hexosyltransferase activity
A	0070417	biological_process	cellular response to cold
B	0003824	molecular_function	catalytic activity
B	0003825	molecular_function	alpha,alpha-trehalose-phosphate synthase (UDP-forming) activity
B	0005992	biological_process	trehalose biosynthetic process
B	0006950	biological_process	response to stress
B	0006970	biological_process	response to osmotic stress
B	0006974	biological_process	DNA damage response
B	0016740	molecular_function	transferase activity
B	0016757	molecular_function	glycosyltransferase activity
B	0016758	molecular_function	hexosyltransferase activity
B	0070417	biological_process	cellular response to cold
C	0003824	molecular_function	catalytic activity
C	0003825	molecular_function	alpha,alpha-trehalose-phosphate synthase (UDP-forming) activity
C	0005992	biological_process	trehalose biosynthetic process
C	0006950	biological_process	response to stress
C	0006970	biological_process	response to osmotic stress
C	0006974	biological_process	DNA damage response
C	0016740	molecular_function	transferase activity
C	0016757	molecular_function	glycosyltransferase activity
C	0016758	molecular_function	hexosyltransferase activity
C	0070417	biological_process	cellular response to cold
D	0003824	molecular_function	catalytic activity
D	0003825	molecular_function	alpha,alpha-trehalose-phosphate synthase (UDP-forming) activity
D	0005992	biological_process	trehalose biosynthetic process
D	0006950	biological_process	response to stress
D	0006970	biological_process	response to osmotic stress
D	0006974	biological_process	DNA damage response
D	0016740	molecular_function	transferase activity
D	0016757	molecular_function	glycosyltransferase activity
D	0016758	molecular_function	hexosyltransferase activity
D	0070417	biological_process	cellular response to cold

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE EDO A 1457

Chain	Residue
A	THR298
A	SER299
A	ARG300
A	GLY301
A	HOH2196
A	HOH2201

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE EDO B 1459

Chain	Residue
B	PRO402
B	TYR403
B	ARG405
A	PHE97
A	HOH2041
B	GLU271

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE EDO A 1458

Chain	Residue
A	HIS89
A	ARG91
A	LEU359
A	TYR403
A	HOH2036
A	HOH2100

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE EDO A 1459

Chain	Residue
A	ASP180
A	ALA217
A	PHE218
A	ARG219
A	ILE453

site_id	AC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE EDO B 1460

Chain	Residue
B	ASN77
B	ARG300
B	GLY301
B	ASP302
B	HOH2147

site_id	AC6
Number of Residues	19
Details	BINDING SITE FOR RESIDUE UDP A 1460

Chain	Residue
A	ALA20
A	GLY21
A	GLY22
A	VAL25
A	VAL260
A	ARG262
A	LYS267
A	HIS338
A	PHE339
A	ARG341
A	LEU344
A	ASN364
A	LEU365
A	VAL366
A	GLU369
A	VDO1461
A	HOH2197
A	HOH2198
A	HOH2199

site_id	AC7
Number of Residues	26
Details	BINDING SITE FOR RESIDUE VDO A 1461

Chain	Residue
A	ARG9
A	GLY22
A	LEU23
A	TYR76
A	TRP85
A	ASP130
A	HIS132
A	HIS154
A	ILE155
A	GLN185
A	ILE225
A	ARG262
A	ARG300
A	ASP361
A	GLY362
A	MET363
A	ASN364
A	LEU365
A	UDP1460
A	HOH2005
A	HOH2013
A	HOH2015
A	HOH2033
A	HOH2200
A	HOH2201
A	HOH2202

site_id	AC8
Number of Residues	17
Details	BINDING SITE FOR RESIDUE UDP B 1461

Chain	Residue
B	ALA20
B	GLY21
B	GLY22
B	VAL260
B	ARG262
B	LYS267
B	HIS338
B	PHE339
B	ARG341
B	LEU344
B	ASN364
B	LEU365
B	VAL366
B	GLU369
B	VDO1462
B	HOH2148
B	HOH2149

site_id	AC9
Number of Residues	26
Details	BINDING SITE FOR RESIDUE VDO B 1462

Chain	Residue
B	HIS132
B	HIS154
B	ILE155
B	ILE225
B	ARG262
B	ARG300
B	ASP361
B	GLY362
B	MET363
B	ASN364
B	LEU365
B	UDP1461
B	HOH2010
B	HOH2030
B	HOH2150
B	HOH2151
B	HOH2152
B	ARG9
B	ALA20
B	GLY21
B	GLY22
B	LEU23
B	TYR76
B	TRP85
B	ASP130
B	TYR131

site_id	BC1
Number of Residues	14
Details	BINDING SITE FOR RESIDUE UDP C 1457

Chain	Residue
C	VAL260
C	ARG262
C	LYS267
C	HIS338
C	PHE339
C	ARG341
C	LEU344
C	ASN364
C	LEU365
C	VAL366
C	GLU369
C	VDO1458
C	HOH2073
C	HOH2074

site_id	BC2
Number of Residues	14
Details	BINDING SITE FOR RESIDUE VDO C 1458

Chain	Residue
C	ASP130
C	HIS154
C	GLN185
C	ILE225
C	ARG262
C	ARG300
C	ASP361
C	GLY362
C	MET363
C	ASN364
C	LEU365
C	UDP1457
C	HOH2057
C	HOH2075

site_id	BC3
Number of Residues	18
Details	BINDING SITE FOR RESIDUE UDP D 1458

Chain	Residue
D	VAL260
D	ARG262
D	LYS267
D	HIS338
D	PHE339
D	ARG341
D	LEU344
D	ASN364
D	LEU365
D	VAL366
D	GLU369
D	VDO1459
D	HOH2145
D	HOH2147
D	HOH2148
D	HOH2149
D	HOH2151
D	HOH2152

site_id	BC4
Number of Residues	17
Details	BINDING SITE FOR RESIDUE VDO D 1459

Chain	Residue
D	TRP85
D	ASP130
D	HIS132
D	HIS154
D	ILE155
D	ILE225
D	ARG262
D	ARG300
D	ASP361
D	GLY362
D	MET363
D	ASN364
D	LEU365
D	UDP1458
D	HOH2153
D	HOH2154
D	HOH2155

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	16
Details	Binding site: {"evidences":[{"source":"PubMed","id":"12498887","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20077550","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1GZ5","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2WTX","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	3
Details	Binding site: {"evidences":[{"source":"PubMed","id":"12498887","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"14570926","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"20077550","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"1GZ5","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2WTX","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	28
Details	Binding site: {"evidences":[{"source":"PubMed","id":"12498887","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"14570926","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"20077550","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"1GZ5","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1UQT","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1UQU","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2WTX","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	8
Details	Site: {"description":"Involved in alpha anomer selectivity","evidences":[{"source":"PubMed","id":"12498887","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	2
Details	M-CSA 622

Chain	Residue	Details
A	HIS154	electrostatic stabiliser
A	ASP361	electrostatic stabiliser

site_id	MCSA2
Number of Residues	2
Details	M-CSA 622

Chain	Residue	Details
B	HIS154	electrostatic stabiliser
B	ASP361	electrostatic stabiliser

site_id	MCSA3
Number of Residues	2
Details	M-CSA 622

Chain	Residue	Details
C	HIS154	electrostatic stabiliser
C	ASP361	electrostatic stabiliser

site_id	MCSA4
Number of Residues	2
Details	M-CSA 622

Chain	Residue	Details
D	HIS154	electrostatic stabiliser
D	ASP361	electrostatic stabiliser

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