Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

7C8I

Ambient temperature structure of Bifidobacgterium longum phosphoketolase with thiamine diphosphate and phosphoenol pyuruvate

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	8
Details	binding site for residue PEP A 901

Chain	Residue
A	SER440
A	TYR501
A	HIS548
A	ASN549
A	LYS605
A	HOH1001
A	HOH1096
B	HIS64

site_id	AC2
Number of Residues	22
Details	binding site for residue TPP A 902

Chain	Residue
A	HIS97
A	GLY155
A	LEU157
A	GLY181
A	ASP182
A	GLY183
A	GLU184
A	ASN215
A	TYR217
A	LYS218
A	ILE219
A	LYS300
A	HIS320
A	CA903
A	HOH1030
A	HOH1105
B	ASP436
B	GLU437
B	LEU477
B	GLU479
B	PHE504
A	THR67

site_id	AC3
Number of Residues	5
Details	binding site for residue CA A 903

Chain	Residue
A	ASP182
A	ASN215
A	TYR217
A	TPP902
A	HOH1030

site_id	AC4
Number of Residues	10
Details	binding site for residue PEP B 901

Chain	Residue
A	HIS64
A	GLN321
A	HOH1130
B	SER440
B	TYR501
B	HIS548
B	ASN549
B	LYS605
B	HOH1003
B	HOH1063

site_id	AC5
Number of Residues	24
Details	binding site for residue TPP B 902

Chain	Residue
A	ASP436
A	GLU437
A	LEU477
A	GLU479
A	PHE504
A	HOH1062
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	CA903
B	HOH1009
B	HOH1172

site_id	AC6
Number of Residues	5
Details	binding site for residue CA B 903

Chain	Residue
B	ASP182
B	ASN215
B	TYR217
B	TPP902
B	HOH1009

site_id	AC7
Number of Residues	9
Details	binding site for residue PEP C 901

Chain	Residue
C	SER440
C	ARG442
C	TYR501
C	HIS548
C	ASN549
C	LYS605
C	HOH1002
D	HIS64
D	GLN321

site_id	AC8
Number of Residues	22
Details	binding site for residue TPP C 902

Chain	Residue
C	HOH1035
D	ASP436
D	GLU437
D	LEU477
D	GLU479
D	PHE504
C	THR67
C	PRO95
C	HIS97
C	GLY155
C	LEU157
C	GLY181
C	GLY183
C	GLU184
C	ASN215
C	TYR217
C	LYS218
C	ILE219
C	LYS300
C	HIS320
C	CA903
C	HOH1017

site_id	AC9
Number of Residues	5
Details	binding site for residue CA C 903

Chain	Residue
C	ASP182
C	ASN215
C	TYR217
C	TPP902
C	HOH1017

site_id	AD1
Number of Residues	8
Details	binding site for residue PEP D 901

Chain	Residue
C	HIS64
C	GLN321
D	SER440
D	ARG442
D	TYR501
D	HIS548
D	ASN549
D	LYS605

site_id	AD2
Number of Residues	20
Details	binding site for residue TPP D 902

Chain	Residue
C	ASP436
C	GLU437
C	LEU477
C	GLU479
C	PHE504
D	THR67
D	HIS97
D	GLY155
D	LEU157
D	GLY181
D	ASP182
D	GLY183
D	GLU184
D	ASN215
D	TYR217
D	LYS218
D	ILE219
D	LYS300
D	HIS320
D	CA903

site_id	AD3
Number of Residues	5
Details	binding site for residue CA D 903

Chain	Residue
D	ASP182
D	HIS213
D	ASN215
D	TYR217
D	TPP902

site_id	AD4
Number of Residues	8
Details	binding site for residue PEP E 901

Chain	Residue
E	SER440
E	ARG442
E	TYR501
E	HIS548
E	ASN549
E	LYS605
F	HIS64
F	GLN321

site_id	AD5
Number of Residues	22
Details	binding site for residue TPP E 902

Chain	Residue
E	THR67
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	CA903
E	HOH1072
F	ASP436
F	GLU437
F	LEU477
F	GLU479
F	PHE504
F	HOH1078

site_id	AD6
Number of Residues	5
Details	binding site for residue CA E 903

Chain	Residue
E	ASP182
E	HIS213
E	ASN215
E	TYR217
E	TPP902

site_id	AD7
Number of Residues	7
Details	binding site for residue PEP F 901

Chain	Residue
E	HIS64
F	SER440
F	TYR501
F	HIS548
F	ASN549
F	LYS605
F	HOH1078

site_id	AD8
Number of Residues	23
Details	binding site for residue TPP F 902

Chain	Residue
E	ASP436
E	GLU437
E	LEU477
E	GLU479
E	PHE504
F	THR67
F	PRO95
F	HIS97
F	GLY155
F	GLU156
F	LEU157
F	GLY181
F	ASP182
F	GLY183
F	GLU184
F	ASN215
F	TYR217
F	LYS218
F	ILE219
F	LYS300
F	HIS320
F	CA903
F	HOH1019

site_id	AD9
Number of Residues	5
Details	binding site for residue CA F 903

Chain	Residue
F	ASP182
F	ASN215
F	TYR217
F	TPP902
F	HOH1019

site_id	AE1
Number of Residues	6
Details	binding site for residue PEP G 901

Chain	Residue
G	SER440
G	ARG442
G	TYR501
G	HIS548
G	ASN549
G	LYS605

site_id	AE2
Number of Residues	25
Details	binding site for residue TPP G 902

Chain	Residue
G	THR67
G	PRO95
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	CA903
G	HOH1078
G	HOH1121
H	ASP436
H	GLU437
H	LEU477
H	GLU479
H	PHE504
H	HOH1058

site_id	AE3
Number of Residues	5
Details	binding site for residue CA G 903

Chain	Residue
G	ASP182
G	ASN215
G	TYR217
G	TPP902
G	HOH1078

site_id	AE4
Number of Residues	7
Details	binding site for residue PEP H 901

Chain	Residue
G	HIS64
H	SER440
H	TYR501
H	HIS548
H	ASN549
H	LYS605
H	HOH1058

site_id	AE5
Number of Residues	21
Details	binding site for residue TPP H 902

Chain	Residue
G	ASP436
G	GLU437
G	LEU477
G	GLU479
G	PHE504
H	THR67
H	PRO95
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	CA903

site_id	AE6
Number of Residues	4
Details	binding site for residue CA H 903

Chain	Residue
H	ASP182
H	ASN215
H	TYR217
H	TPP902

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)