Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3HN6

Crystal structure of glucosamine-6-phosphate deaminase from Borrelia burgdorferi

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0004342	molecular_function	glucosamine-6-phosphate deaminase activity
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0005975	biological_process	carbohydrate metabolic process
A	0006043	biological_process	glucosamine catabolic process
A	0006044	biological_process	N-acetylglucosamine metabolic process
A	0006046	biological_process	N-acetylglucosamine catabolic process
A	0016787	molecular_function	hydrolase activity
A	0019262	biological_process	N-acetylneuraminate catabolic process
A	0042802	molecular_function	identical protein binding
B	0003824	molecular_function	catalytic activity
B	0004342	molecular_function	glucosamine-6-phosphate deaminase activity
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0005975	biological_process	carbohydrate metabolic process
B	0006043	biological_process	glucosamine catabolic process
B	0006044	biological_process	N-acetylglucosamine metabolic process
B	0006046	biological_process	N-acetylglucosamine catabolic process
B	0016787	molecular_function	hydrolase activity
B	0019262	biological_process	N-acetylneuraminate catabolic process
B	0042802	molecular_function	identical protein binding
C	0003824	molecular_function	catalytic activity
C	0004342	molecular_function	glucosamine-6-phosphate deaminase activity
C	0005737	cellular_component	cytoplasm
C	0005829	cellular_component	cytosol
C	0005975	biological_process	carbohydrate metabolic process
C	0006043	biological_process	glucosamine catabolic process
C	0006044	biological_process	N-acetylglucosamine metabolic process
C	0006046	biological_process	N-acetylglucosamine catabolic process
C	0016787	molecular_function	hydrolase activity
C	0019262	biological_process	N-acetylneuraminate catabolic process
C	0042802	molecular_function	identical protein binding
D	0003824	molecular_function	catalytic activity
D	0004342	molecular_function	glucosamine-6-phosphate deaminase activity
D	0005737	cellular_component	cytoplasm
D	0005829	cellular_component	cytosol
D	0005975	biological_process	carbohydrate metabolic process
D	0006043	biological_process	glucosamine catabolic process
D	0006044	biological_process	N-acetylglucosamine metabolic process
D	0006046	biological_process	N-acetylglucosamine catabolic process
D	0016787	molecular_function	hydrolase activity
D	0019262	biological_process	N-acetylneuraminate catabolic process
D	0042802	molecular_function	identical protein binding
E	0003824	molecular_function	catalytic activity
E	0004342	molecular_function	glucosamine-6-phosphate deaminase activity
E	0005737	cellular_component	cytoplasm
E	0005829	cellular_component	cytosol
E	0005975	biological_process	carbohydrate metabolic process
E	0006043	biological_process	glucosamine catabolic process
E	0006044	biological_process	N-acetylglucosamine metabolic process
E	0006046	biological_process	N-acetylglucosamine catabolic process
E	0016787	molecular_function	hydrolase activity
E	0019262	biological_process	N-acetylneuraminate catabolic process
E	0042802	molecular_function	identical protein binding
F	0003824	molecular_function	catalytic activity
F	0004342	molecular_function	glucosamine-6-phosphate deaminase activity
F	0005737	cellular_component	cytoplasm
F	0005829	cellular_component	cytosol
F	0005975	biological_process	carbohydrate metabolic process
F	0006043	biological_process	glucosamine catabolic process
F	0006044	biological_process	N-acetylglucosamine metabolic process
F	0006046	biological_process	N-acetylglucosamine catabolic process
F	0016787	molecular_function	hydrolase activity
F	0019262	biological_process	N-acetylneuraminate catabolic process
F	0042802	molecular_function	identical protein binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	8
Details	BINDING SITE FOR RESIDUE POP B 303

Chain	Residue
A	ARG210
A	LYS213
A	HIS214
B	ARG210
B	LYS213
B	HIS214
B	HOH742
B	HOH743

site_id	AC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE POP C 302

Chain	Residue
C	LYS213
C	HIS214
C	HOH820
F	ARG210
F	LYS213
F	HIS214
C	ARG210

site_id	AC3
Number of Residues	7
Details	BINDING SITE FOR RESIDUE POP D 301

Chain	Residue
D	ARG210
D	LYS213
D	HIS214
E	ARG210
E	LYS213
E	HIS214
E	LYS218

Functional Information from PROSITE/UniProt

site_id	PS01161
Number of Residues	19
Details	GLC_GALNAC_ISOMERASE Glucosamine/galactosamine-6-phosphate isomerases signature. IksfGgImLfVgGIGpDGH

Chain	Residue	Details
A	ILE125-HIS143

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	6
Details	ACT_SITE: Proton acceptor; for enolization step => ECO:0000250

Chain	Residue	Details
A	ASP72
B	ASP72
C	ASP72
D	ASP72
E	ASP72
F	ASP72

site_id	SWS_FT_FI2
Number of Residues	12
Details	ACT_SITE: For ring-opening step => ECO:0000250

Chain	Residue	Details
A	ASP141
E	GLU148
F	ASP141
F	GLU148
A	GLU148
B	ASP141
B	GLU148
C	ASP141
C	GLU148
D	ASP141
D	GLU148
E	ASP141

site_id	SWS_FT_FI3
Number of Residues	6
Details	ACT_SITE: Proton acceptor; for ring-opening step => ECO:0000250

Chain	Residue	Details
A	HIS143
B	HIS143
C	HIS143
D	HIS143
E	HIS143
F	HIS143

site_id	SWS_FT_FI4
Number of Residues	30
Details	SITE: Part of the allosteric site => ECO:0000250

Chain	Residue	Details
A	SER151
B	TYR254
C	SER151
C	ARG158
C	LYS160
C	THR161
C	TYR254
D	SER151
D	ARG158
D	LYS160
D	THR161
A	ARG158
D	TYR254
E	SER151
E	ARG158
E	LYS160
E	THR161
E	TYR254
F	SER151
F	ARG158
F	LYS160
F	THR161
A	LYS160
F	TYR254
A	THR161
A	TYR254
B	SER151
B	ARG158
B	LYS160
B	THR161

Catalytic Information from CSA

site_id	CSA1
Number of Residues	4
Details	Annotated By Reference To The Literature 1cd5

Chain	Residue	Details
A	HIS143
A	GLU148
A	ASP141
A	ASP72

site_id	CSA2
Number of Residues	4
Details	Annotated By Reference To The Literature 1cd5

Chain	Residue	Details
B	HIS143
B	GLU148
B	ASP141
B	ASP72

site_id	CSA3
Number of Residues	4
Details	Annotated By Reference To The Literature 1cd5

Chain	Residue	Details
C	HIS143
C	GLU148
C	ASP141
C	ASP72

site_id	CSA4
Number of Residues	4
Details	Annotated By Reference To The Literature 1cd5

Chain	Residue	Details
D	HIS143
D	GLU148
D	ASP141
D	ASP72

site_id	CSA5
Number of Residues	4
Details	Annotated By Reference To The Literature 1cd5

Chain	Residue	Details
E	HIS143
E	GLU148
E	ASP141
E	ASP72

site_id	CSA6
Number of Residues	4
Details	Annotated By Reference To The Literature 1cd5

Chain	Residue	Details
F	HIS143
F	GLU148
F	ASP141
F	ASP72

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