Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3EUA

CRYSTAL STRUCTURE OF A PUTATIVE PHOSPHOSUGAR ISOMERASE (BSU32610) FROM BACILLUS SUBTILIS AT 1.90 A RESOLUTION

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004360	molecular_function	glutamine-fructose-6-phosphate transaminase (isomerizing) activity
A	0006002	biological_process	fructose 6-phosphate metabolic process
A	0006047	biological_process	UDP-N-acetylglucosamine metabolic process
A	0006487	biological_process	protein N-linked glycosylation
A	0016787	molecular_function	hydrolase activity
A	0097367	molecular_function	carbohydrate derivative binding
A	1901135	biological_process	carbohydrate derivative metabolic process
B	0004360	molecular_function	glutamine-fructose-6-phosphate transaminase (isomerizing) activity
B	0006002	biological_process	fructose 6-phosphate metabolic process
B	0006047	biological_process	UDP-N-acetylglucosamine metabolic process
B	0006487	biological_process	protein N-linked glycosylation
B	0016787	molecular_function	hydrolase activity
B	0097367	molecular_function	carbohydrate derivative binding
B	1901135	biological_process	carbohydrate derivative metabolic process
C	0004360	molecular_function	glutamine-fructose-6-phosphate transaminase (isomerizing) activity
C	0006002	biological_process	fructose 6-phosphate metabolic process
C	0006047	biological_process	UDP-N-acetylglucosamine metabolic process
C	0006487	biological_process	protein N-linked glycosylation
C	0016787	molecular_function	hydrolase activity
C	0097367	molecular_function	carbohydrate derivative binding
C	1901135	biological_process	carbohydrate derivative metabolic process
D	0004360	molecular_function	glutamine-fructose-6-phosphate transaminase (isomerizing) activity
D	0006002	biological_process	fructose 6-phosphate metabolic process
D	0006047	biological_process	UDP-N-acetylglucosamine metabolic process
D	0006487	biological_process	protein N-linked glycosylation
D	0016787	molecular_function	hydrolase activity
D	0097367	molecular_function	carbohydrate derivative binding
D	1901135	biological_process	carbohydrate derivative metabolic process
E	0004360	molecular_function	glutamine-fructose-6-phosphate transaminase (isomerizing) activity
E	0006002	biological_process	fructose 6-phosphate metabolic process
E	0006047	biological_process	UDP-N-acetylglucosamine metabolic process
E	0006487	biological_process	protein N-linked glycosylation
E	0016787	molecular_function	hydrolase activity
E	0097367	molecular_function	carbohydrate derivative binding
E	1901135	biological_process	carbohydrate derivative metabolic process
F	0004360	molecular_function	glutamine-fructose-6-phosphate transaminase (isomerizing) activity
F	0006002	biological_process	fructose 6-phosphate metabolic process
F	0006047	biological_process	UDP-N-acetylglucosamine metabolic process
F	0006487	biological_process	protein N-linked glycosylation
F	0016787	molecular_function	hydrolase activity
F	0097367	molecular_function	carbohydrate derivative binding
F	1901135	biological_process	carbohydrate derivative metabolic process
G	0004360	molecular_function	glutamine-fructose-6-phosphate transaminase (isomerizing) activity
G	0006002	biological_process	fructose 6-phosphate metabolic process
G	0006047	biological_process	UDP-N-acetylglucosamine metabolic process
G	0006487	biological_process	protein N-linked glycosylation
G	0016787	molecular_function	hydrolase activity
G	0097367	molecular_function	carbohydrate derivative binding
G	1901135	biological_process	carbohydrate derivative metabolic process
H	0004360	molecular_function	glutamine-fructose-6-phosphate transaminase (isomerizing) activity
H	0006002	biological_process	fructose 6-phosphate metabolic process
H	0006047	biological_process	UDP-N-acetylglucosamine metabolic process
H	0006487	biological_process	protein N-linked glycosylation
H	0016787	molecular_function	hydrolase activity
H	0097367	molecular_function	carbohydrate derivative binding
H	1901135	biological_process	carbohydrate derivative metabolic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	10
Details	BINDING SITE FOR RESIDUE FLC C 329

Chain	Residue
C	SER81
D	HIS233
C	HIS82
C	SER83
C	THR86
C	MSE323
C	TRP324
C	GOL330
C	HOH868
C	HOH1617

site_id	AC2
Number of Residues	10
Details	BINDING SITE FOR RESIDUE FLC H 329

Chain	Residue
G	HIS233
H	SER81
H	HIS82
H	SER83
H	THR86
H	TRP324
H	HOH629
H	HOH674
H	HOH751
H	HOH771

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE GOL H 330

Chain	Residue
H	ASP125
H	TRP126
H	ALA130
H	HOH666

site_id	AC4
Number of Residues	8
Details	BINDING SITE FOR RESIDUE GOL C 330

Chain	Residue
C	GLY33
C	GLY34
C	CYS213
C	GLU217
C	MSE218
C	MSE323
C	FLC329
D	HIS233

Catalytic Information from CSA

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

Chain	Residue	Details
A	HIS233

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

Chain	Residue	Details
B	HIS233

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

Chain	Residue	Details
C	HIS233

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

Chain	Residue	Details
D	HIS233

site_id	CSA5
Number of Residues	1
Details	Annotated By Reference To The Literature 1jxa

Chain	Residue	Details
E	HIS233

site_id	CSA6
Number of Residues	1
Details	Annotated By Reference To The Literature 1jxa

Chain	Residue	Details
F	HIS233

site_id	CSA7
Number of Residues	1
Details	Annotated By Reference To The Literature 1jxa

Chain	Residue	Details
G	HIS233

site_id	CSA8
Number of Residues	1
Details	Annotated By Reference To The Literature 1jxa

Chain	Residue	Details
H	HIS233

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