Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3AI7

Crystal Structure of Bifidobacterium Longum Phosphoketolase

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000287	molecular_function	magnesium ion binding
A	0005975	biological_process	carbohydrate metabolic process
A	0016829	molecular_function	lyase activity
A	0016832	molecular_function	aldehyde-lyase activity
A	0046872	molecular_function	metal ion binding
A	0047905	molecular_function	fructose-6-phosphate phosphoketolase activity
B	0000287	molecular_function	magnesium ion binding
B	0005975	biological_process	carbohydrate metabolic process
B	0016829	molecular_function	lyase activity
B	0016832	molecular_function	aldehyde-lyase activity
B	0046872	molecular_function	metal ion binding
B	0047905	molecular_function	fructose-6-phosphate phosphoketolase activity
C	0000287	molecular_function	magnesium ion binding
C	0005975	biological_process	carbohydrate metabolic process
C	0016829	molecular_function	lyase activity
C	0016832	molecular_function	aldehyde-lyase activity
C	0046872	molecular_function	metal ion binding
C	0047905	molecular_function	fructose-6-phosphate phosphoketolase activity
D	0000287	molecular_function	magnesium ion binding
D	0005975	biological_process	carbohydrate metabolic process
D	0016829	molecular_function	lyase activity
D	0016832	molecular_function	aldehyde-lyase activity
D	0046872	molecular_function	metal ion binding
D	0047905	molecular_function	fructose-6-phosphate phosphoketolase activity
E	0000287	molecular_function	magnesium ion binding
E	0005975	biological_process	carbohydrate metabolic process
E	0016829	molecular_function	lyase activity
E	0016832	molecular_function	aldehyde-lyase activity
E	0046872	molecular_function	metal ion binding
E	0047905	molecular_function	fructose-6-phosphate phosphoketolase activity
F	0000287	molecular_function	magnesium ion binding
F	0005975	biological_process	carbohydrate metabolic process
F	0016829	molecular_function	lyase activity
F	0016832	molecular_function	aldehyde-lyase activity
F	0046872	molecular_function	metal ion binding
F	0047905	molecular_function	fructose-6-phosphate phosphoketolase activity
G	0000287	molecular_function	magnesium ion binding
G	0005975	biological_process	carbohydrate metabolic process
G	0016829	molecular_function	lyase activity
G	0016832	molecular_function	aldehyde-lyase activity
G	0046872	molecular_function	metal ion binding
G	0047905	molecular_function	fructose-6-phosphate phosphoketolase activity
H	0000287	molecular_function	magnesium ion binding
H	0005975	biological_process	carbohydrate metabolic process
H	0016829	molecular_function	lyase activity
H	0016832	molecular_function	aldehyde-lyase activity
H	0046872	molecular_function	metal ion binding
H	0047905	molecular_function	fructose-6-phosphate phosphoketolase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	24
Details	BINDING SITE FOR RESIDUE TPP A 900

Chain	Residue
A	THR67
A	TYR217
A	LYS218
A	ILE219
A	LYS300
A	HIS320
A	HOH870
A	CA901
A	HOH2846
A	HOH5052
B	ASP436
A	HIS97
B	GLU437
B	LEU477
B	GLU479
B	PHE504
B	HOH4638
A	GLY155
A	LEU157
A	GLY181
A	ASP182
A	GLY183
A	GLU184
A	ASN215

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA A 901

Chain	Residue
A	ASP182
A	ASN215
A	TYR217
A	TPP900
A	HOH5052

site_id	AC3
Number of Residues	24
Details	BINDING SITE FOR RESIDUE TPP B 900

Chain	Residue
A	ASP436
A	GLU437
A	LEU477
A	GLU479
A	PHE504
B	THR67
B	HIS97
B	GLY155
B	LEU157
B	GLY181
B	ASP182
B	GLY183
B	GLU184
B	HIS213
B	ASN215
B	TYR217
B	LYS218
B	ILE219
B	LYS300
B	HIS320
B	CA901
B	HOH934
B	HOH953
B	HOH5051

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA B 901

Chain	Residue
B	ASP182
B	ASN215
B	TYR217
B	TPP900
B	HOH5051

site_id	AC5
Number of Residues	23
Details	BINDING SITE FOR RESIDUE TPP C 900

Chain	Residue
C	THR67
C	HIS97
C	GLY155
C	LEU157
C	GLY181
C	ASP182
C	GLY183
C	GLU184
C	ASN215
C	TYR217
C	LYS218
C	ILE219
C	LYS300
C	HIS320
C	CA901
C	HOH942
C	HOH1336
C	HOH5053
D	ASP436
D	GLU437
D	LEU477
D	GLU479
D	PHE504

site_id	AC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA C 901

Chain	Residue
C	ASP182
C	ASN215
C	TYR217
C	TPP900
C	HOH5053

site_id	AC7
Number of Residues	24
Details	BINDING SITE FOR RESIDUE TPP D 900

Chain	Residue
D	GLU184
D	HIS213
D	ASN215
D	TYR217
D	LYS218
D	ILE219
D	LYS300
D	HIS320
D	CA901
D	HOH941
D	HOH1179
C	ASP436
C	GLU437
C	LEU477
C	GLU479
C	PHE504
C	HOH1918
D	THR67
D	HIS97
D	GLY155
D	LEU157
D	GLY181
D	ASP182
D	GLY183

site_id	AC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA D 901

Chain	Residue
D	ASP182
D	ASN215
D	TYR217
D	TPP900
D	HOH1179

site_id	AC9
Number of Residues	25
Details	BINDING SITE FOR RESIDUE TPP E 900

Chain	Residue
E	THR67
E	PRO95
E	HIS97
E	GLY155
E	LEU157
E	GLY181
E	ASP182
E	GLY183
E	GLU184
E	ASN215
E	TYR217
E	LYS218
E	ILE219
E	LYS300
E	HIS320
E	CA901
E	HOH1095
E	HOH1452
E	HOH2468
F	ASP436
F	GLU437
F	LEU477
F	GLU479
F	PHE504
F	HOH3773

site_id	BC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA E 901

Chain	Residue
E	ASP182
E	ASN215
E	TYR217
E	TPP900
E	HOH1452

site_id	BC2
Number of Residues	24
Details	BINDING SITE FOR RESIDUE TPP F 900

Chain	Residue
E	ASP436
E	GLU437
E	LEU477
E	GLU479
E	PHE504
E	HOH2791
F	THR67
F	HIS97
F	GLY155
F	LEU157
F	GLY181
F	ASP182
F	GLY183
F	GLU184
F	ASN215
F	TYR217
F	LYS218
F	ILE219
F	LYS300
F	HIS320
F	CA901
F	HOH1312
F	HOH3470
F	HOH5054

site_id	BC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA F 901

Chain	Residue
F	ASP182
F	ASN215
F	TYR217
F	TPP900
F	HOH5054

site_id	BC4
Number of Residues	24
Details	BINDING SITE FOR RESIDUE TPP G 900

Chain	Residue
G	THR67
G	HIS97
G	GLY155
G	LEU157
G	GLY181
G	ASP182
G	GLY183
G	GLU184
G	HIS213
G	ASN215
G	TYR217
G	LYS218
G	ILE219
G	LYS300
G	HIS320
G	CA901
G	HOH1024
G	HOH3687
G	HOH5056
H	ASP436
H	GLU437
H	LEU477
H	GLU479
H	PHE504

site_id	BC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA G 901

Chain	Residue
G	ASP182
G	ASN215
G	TYR217
G	TPP900
G	HOH5056

site_id	BC6
Number of Residues	23
Details	BINDING SITE FOR RESIDUE TPP H 900

Chain	Residue
G	ASP436
G	GLU437
G	LEU477
G	GLU479
G	PHE504
G	HOH1565
H	THR67
H	HIS97
H	GLY155
H	LEU157
H	GLY181
H	ASP182
H	GLY183
H	GLU184
H	ASN215
H	TYR217
H	LYS218
H	ILE219
H	LYS300
H	HIS320
H	CA901
H	HOH1957
H	HOH5055

site_id	BC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA H 901

Chain	Residue
H	ASP182
H	ASN215
H	TYR217
H	TPP900
H	HOH5055

Functional Information from PROSITE/UniProt

site_id	PS60002
Number of Residues	7
Details	PHOSPHOKETOLASE_1 Phosphoketolase signature 1. EGGELGY

Chain	Residue	Details
A	GLU153-TYR159

site_id	PS60003
Number of Residues	19
Details	PHOSPHOKETOLASE_2 Phosphoketolase signature 2. GaimDnPslFvpaIvGDGE

Chain	Residue	Details
A	GLY166-GLU184

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