4F9F

Crystal Structure of VldE, the pseudo-glycosyltransferase, in complex with GDP and Trehalose

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0005992	biological_process	trehalose biosynthetic process
A	0016740	molecular_function	transferase activity
A	0016758	molecular_function	hexosyltransferase activity
A	0017000	biological_process	antibiotic biosynthetic process
B	0003824	molecular_function	catalytic activity
B	0005992	biological_process	trehalose biosynthetic process
B	0016740	molecular_function	transferase activity
B	0016758	molecular_function	hexosyltransferase activity
B	0017000	biological_process	antibiotic biosynthetic process
C	0003824	molecular_function	catalytic activity
C	0005992	biological_process	trehalose biosynthetic process
C	0016740	molecular_function	transferase activity
C	0016758	molecular_function	hexosyltransferase activity
C	0017000	biological_process	antibiotic biosynthetic process
D	0003824	molecular_function	catalytic activity
D	0005992	biological_process	trehalose biosynthetic process
D	0016740	molecular_function	transferase activity
D	0016758	molecular_function	hexosyltransferase activity
D	0017000	biological_process	antibiotic biosynthetic process
E	0003824	molecular_function	catalytic activity
E	0005992	biological_process	trehalose biosynthetic process
E	0016740	molecular_function	transferase activity
E	0016758	molecular_function	hexosyltransferase activity
E	0017000	biological_process	antibiotic biosynthetic process
F	0003824	molecular_function	catalytic activity
F	0005992	biological_process	trehalose biosynthetic process
F	0016740	molecular_function	transferase activity
F	0016758	molecular_function	hexosyltransferase activity
F	0017000	biological_process	antibiotic biosynthetic process

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	18
Details	BINDING: BINDING => ECO:0000305|PubMed:23028689, ECO:0007744|PDB:4F97

Chain	Residue	Details
A	ASP158
D	ASP158
D	HIS182
D	ASN325
E	ASP158
E	HIS182
E	ASN325
F	ASP158
F	HIS182
F	ASN325
A	HIS182
A	ASN325
B	ASP158
B	HIS182
B	ASN325
C	ASP158
C	HIS182
C	ASN325

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site_id	SWS_FT_FI2
Number of Residues	36
Details	BINDING: BINDING => ECO:0000305|PubMed:23028689, ECO:0007744|PDB:4F96, ECO:0007744|PDB:4F97, ECO:0007744|PDB:4F9F

Chain	Residue	Details
A	ARG290
B	THR366
B	LEU387
B	GLU391
C	ARG290
C	LYS295
C	ASN361
C	THR366
C	LEU387
C	GLU391
D	ARG290
A	LYS295
D	LYS295
D	ASN361
D	THR366
D	LEU387
D	GLU391
E	ARG290
E	LYS295
E	ASN361
E	THR366
E	LEU387
A	ASN361
E	GLU391
F	ARG290
F	LYS295
F	ASN361
F	THR366
F	LEU387
F	GLU391
A	THR366
A	LEU387
A	GLU391
B	ARG290
B	LYS295
B	ASN361

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site_id	SWS_FT_FI3
Number of Residues	12
Details	BINDING: BINDING => ECO:0000305|PubMed:23028689, ECO:0007744|PDB:4F97, ECO:0007744|PDB:4F9F

Chain	Residue	Details
A	ARG321
E	ASP383
F	ARG321
F	ASP383
A	ASP383
B	ARG321
B	ASP383
C	ARG321
C	ASP383
D	ARG321
D	ASP383
E	ARG321

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