5LQD

Trehalose-6-phosphate synthase, GDP-glucose-dependent OtsA

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	0004805	molecular_function	trehalose-phosphatase activity
A	0005829	cellular_component	cytosol
A	0005992	biological_process	trehalose biosynthetic process
A	0016757	molecular_function	glycosyltransferase activity
A	0016758	molecular_function	hexosyltransferase activity
A	0070413	biological_process	trehalose metabolism in response to stress
B	0003824	molecular_function	catalytic activity
B	0003825	molecular_function	alpha,alpha-trehalose-phosphate synthase (UDP-forming) activity
B	0004805	molecular_function	trehalose-phosphatase activity
B	0005829	cellular_component	cytosol
B	0005992	biological_process	trehalose biosynthetic process
B	0016757	molecular_function	glycosyltransferase activity
B	0016758	molecular_function	hexosyltransferase activity
B	0070413	biological_process	trehalose metabolism in response to stress
C	0003824	molecular_function	catalytic activity
C	0003825	molecular_function	alpha,alpha-trehalose-phosphate synthase (UDP-forming) activity
C	0004805	molecular_function	trehalose-phosphatase activity
C	0005829	cellular_component	cytosol
C	0005992	biological_process	trehalose biosynthetic process
C	0016757	molecular_function	glycosyltransferase activity
C	0016758	molecular_function	hexosyltransferase activity
C	0070413	biological_process	trehalose metabolism in response to stress
D	0003824	molecular_function	catalytic activity
D	0003825	molecular_function	alpha,alpha-trehalose-phosphate synthase (UDP-forming) activity
D	0004805	molecular_function	trehalose-phosphatase activity
D	0005829	cellular_component	cytosol
D	0005992	biological_process	trehalose biosynthetic process
D	0016757	molecular_function	glycosyltransferase activity
D	0016758	molecular_function	hexosyltransferase activity
D	0070413	biological_process	trehalose metabolism in response to stress

Functional Information from PDB Data

site_id	AC1
Number of Residues	8
Details	binding site for residue MES A 1000

Chain	Residue
A	ASN87
A	TRP91
A	GLU265
A	LYS268
A	SER300
A	HOH1148
A	HOH1171
A	HOH1216

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site_id	AC2
Number of Residues	4
Details	binding site for residue EDO A 1001

Chain	Residue
A	PRO104
A	VAL105
A	ARG113
A	VAL89

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site_id	AC3
Number of Residues	8
Details	binding site for residue MES B 1000

Chain	Residue
B	ASN87
B	TRP91
B	GLU265
B	LYS268
B	SER300
B	HOH1112
B	HOH1121
B	HOH1158

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site_id	AC4
Number of Residues	4
Details	binding site for residue EDO B 1001

Chain	Residue
B	VAL89
B	PRO104
B	VAL105
B	ARG113

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site_id	AC5
Number of Residues	10
Details	binding site for residue MES C 1000

Chain	Residue
C	ASN87
C	TRP91
C	ARG263
C	GLU265
C	LYS268
C	SER300
C	HOH1142
C	HOH1165
C	HOH1196
C	HOH1207

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site_id	AC6
Number of Residues	8
Details	binding site for residue EDO C 1001

Chain	Residue
C	VAL89
C	TYR98
C	PRO104
C	VAL105
C	PHE106
C	PHE110
C	HOH1131
C	HOH1133

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site_id	AC7
Number of Residues	10
Details	binding site for residue MES D 1000

Chain	Residue
D	ASN87
D	TRP91
D	ARG263
D	GLU265
D	LYS268
D	SER300
D	HOH1128
D	HOH1140
D	HOH1177
D	HOH1200

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site_id	AC8
Number of Residues	5
Details	binding site for residue EDO D 1001

Chain	Residue
D	VAL89
D	TYR98
D	PRO104
D	VAL105
D	HOH1122

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Functional Information from PROSITE/UniProt

site_id	PS00276
Number of Residues	12
Details	CHANNEL_COLICIN Channel forming colicins signature. TadWqPVLVsvE

Chain	Residue	Details
A	THR327-GLU338

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