Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

5L6V

Crystal structure of E. coli ADP-glucose pyrophosphorylase (AGPase) in complex with a negative allosteric regulator adenosine monophosphate (AMP) - AGPase*AMP

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000287	molecular_function	magnesium ion binding
A	0005524	molecular_function	ATP binding
A	0005978	biological_process	glycogen biosynthetic process
A	0008878	molecular_function	glucose-1-phosphate adenylyltransferase activity
A	0009058	biological_process	biosynthetic process
A	0010170	cellular_component	glucose-1-phosphate adenylyltransferase complex
A	0016208	molecular_function	AMP binding
A	0016779	molecular_function	nucleotidyltransferase activity
A	0042802	molecular_function	identical protein binding
A	0051289	biological_process	protein homotetramerization
B	0000287	molecular_function	magnesium ion binding
B	0005524	molecular_function	ATP binding
B	0005978	biological_process	glycogen biosynthetic process
B	0008878	molecular_function	glucose-1-phosphate adenylyltransferase activity
B	0009058	biological_process	biosynthetic process
B	0010170	cellular_component	glucose-1-phosphate adenylyltransferase complex
B	0016208	molecular_function	AMP binding
B	0016779	molecular_function	nucleotidyltransferase activity
B	0042802	molecular_function	identical protein binding
B	0051289	biological_process	protein homotetramerization
C	0000287	molecular_function	magnesium ion binding
C	0005524	molecular_function	ATP binding
C	0005978	biological_process	glycogen biosynthetic process
C	0008878	molecular_function	glucose-1-phosphate adenylyltransferase activity
C	0009058	biological_process	biosynthetic process
C	0010170	cellular_component	glucose-1-phosphate adenylyltransferase complex
C	0016208	molecular_function	AMP binding
C	0016779	molecular_function	nucleotidyltransferase activity
C	0042802	molecular_function	identical protein binding
C	0051289	biological_process	protein homotetramerization
D	0000287	molecular_function	magnesium ion binding
D	0005524	molecular_function	ATP binding
D	0005978	biological_process	glycogen biosynthetic process
D	0008878	molecular_function	glucose-1-phosphate adenylyltransferase activity
D	0009058	biological_process	biosynthetic process
D	0010170	cellular_component	glucose-1-phosphate adenylyltransferase complex
D	0016208	molecular_function	AMP binding
D	0016779	molecular_function	nucleotidyltransferase activity
D	0042802	molecular_function	identical protein binding
D	0051289	biological_process	protein homotetramerization
E	0000287	molecular_function	magnesium ion binding
E	0005524	molecular_function	ATP binding
E	0005978	biological_process	glycogen biosynthetic process
E	0008878	molecular_function	glucose-1-phosphate adenylyltransferase activity
E	0009058	biological_process	biosynthetic process
E	0010170	cellular_component	glucose-1-phosphate adenylyltransferase complex
E	0016208	molecular_function	AMP binding
E	0016779	molecular_function	nucleotidyltransferase activity
E	0042802	molecular_function	identical protein binding
E	0051289	biological_process	protein homotetramerization
F	0000287	molecular_function	magnesium ion binding
F	0005524	molecular_function	ATP binding
F	0005978	biological_process	glycogen biosynthetic process
F	0008878	molecular_function	glucose-1-phosphate adenylyltransferase activity
F	0009058	biological_process	biosynthetic process
F	0010170	cellular_component	glucose-1-phosphate adenylyltransferase complex
F	0016208	molecular_function	AMP binding
F	0016779	molecular_function	nucleotidyltransferase activity
F	0042802	molecular_function	identical protein binding
F	0051289	biological_process	protein homotetramerization
G	0000287	molecular_function	magnesium ion binding
G	0005524	molecular_function	ATP binding
G	0005978	biological_process	glycogen biosynthetic process
G	0008878	molecular_function	glucose-1-phosphate adenylyltransferase activity
G	0009058	biological_process	biosynthetic process
G	0010170	cellular_component	glucose-1-phosphate adenylyltransferase complex
G	0016208	molecular_function	AMP binding
G	0016779	molecular_function	nucleotidyltransferase activity
G	0042802	molecular_function	identical protein binding
G	0051289	biological_process	protein homotetramerization
H	0000287	molecular_function	magnesium ion binding
H	0005524	molecular_function	ATP binding
H	0005978	biological_process	glycogen biosynthetic process
H	0008878	molecular_function	glucose-1-phosphate adenylyltransferase activity
H	0009058	biological_process	biosynthetic process
H	0010170	cellular_component	glucose-1-phosphate adenylyltransferase complex
H	0016208	molecular_function	AMP binding
H	0016779	molecular_function	nucleotidyltransferase activity
H	0042802	molecular_function	identical protein binding
H	0051289	biological_process	protein homotetramerization
I	0000287	molecular_function	magnesium ion binding
I	0005524	molecular_function	ATP binding
I	0005978	biological_process	glycogen biosynthetic process
I	0008878	molecular_function	glucose-1-phosphate adenylyltransferase activity
I	0009058	biological_process	biosynthetic process
I	0010170	cellular_component	glucose-1-phosphate adenylyltransferase complex
I	0016208	molecular_function	AMP binding
I	0016779	molecular_function	nucleotidyltransferase activity
I	0042802	molecular_function	identical protein binding
I	0051289	biological_process	protein homotetramerization
J	0000287	molecular_function	magnesium ion binding
J	0005524	molecular_function	ATP binding
J	0005978	biological_process	glycogen biosynthetic process
J	0008878	molecular_function	glucose-1-phosphate adenylyltransferase activity
J	0009058	biological_process	biosynthetic process
J	0010170	cellular_component	glucose-1-phosphate adenylyltransferase complex
J	0016208	molecular_function	AMP binding
J	0016779	molecular_function	nucleotidyltransferase activity
J	0042802	molecular_function	identical protein binding
J	0051289	biological_process	protein homotetramerization
K	0000287	molecular_function	magnesium ion binding
K	0005524	molecular_function	ATP binding
K	0005978	biological_process	glycogen biosynthetic process
K	0008878	molecular_function	glucose-1-phosphate adenylyltransferase activity
K	0009058	biological_process	biosynthetic process
K	0010170	cellular_component	glucose-1-phosphate adenylyltransferase complex
K	0016208	molecular_function	AMP binding
K	0016779	molecular_function	nucleotidyltransferase activity
K	0042802	molecular_function	identical protein binding
K	0051289	biological_process	protein homotetramerization
L	0000287	molecular_function	magnesium ion binding
L	0005524	molecular_function	ATP binding
L	0005978	biological_process	glycogen biosynthetic process
L	0008878	molecular_function	glucose-1-phosphate adenylyltransferase activity
L	0009058	biological_process	biosynthetic process
L	0010170	cellular_component	glucose-1-phosphate adenylyltransferase complex
L	0016208	molecular_function	AMP binding
L	0016779	molecular_function	nucleotidyltransferase activity
L	0042802	molecular_function	identical protein binding
L	0051289	biological_process	protein homotetramerization
M	0000287	molecular_function	magnesium ion binding
M	0005524	molecular_function	ATP binding
M	0005978	biological_process	glycogen biosynthetic process
M	0008878	molecular_function	glucose-1-phosphate adenylyltransferase activity
M	0009058	biological_process	biosynthetic process
M	0010170	cellular_component	glucose-1-phosphate adenylyltransferase complex
M	0016208	molecular_function	AMP binding
M	0016779	molecular_function	nucleotidyltransferase activity
M	0042802	molecular_function	identical protein binding
M	0051289	biological_process	protein homotetramerization
N	0000287	molecular_function	magnesium ion binding
N	0005524	molecular_function	ATP binding
N	0005978	biological_process	glycogen biosynthetic process
N	0008878	molecular_function	glucose-1-phosphate adenylyltransferase activity
N	0009058	biological_process	biosynthetic process
N	0010170	cellular_component	glucose-1-phosphate adenylyltransferase complex
N	0016208	molecular_function	AMP binding
N	0016779	molecular_function	nucleotidyltransferase activity
N	0042802	molecular_function	identical protein binding
N	0051289	biological_process	protein homotetramerization
O	0000287	molecular_function	magnesium ion binding
O	0005524	molecular_function	ATP binding
O	0005978	biological_process	glycogen biosynthetic process
O	0008878	molecular_function	glucose-1-phosphate adenylyltransferase activity
O	0009058	biological_process	biosynthetic process
O	0010170	cellular_component	glucose-1-phosphate adenylyltransferase complex
O	0016208	molecular_function	AMP binding
O	0016779	molecular_function	nucleotidyltransferase activity
O	0042802	molecular_function	identical protein binding
O	0051289	biological_process	protein homotetramerization
P	0000287	molecular_function	magnesium ion binding
P	0005524	molecular_function	ATP binding
P	0005978	biological_process	glycogen biosynthetic process
P	0008878	molecular_function	glucose-1-phosphate adenylyltransferase activity
P	0009058	biological_process	biosynthetic process
P	0010170	cellular_component	glucose-1-phosphate adenylyltransferase complex
P	0016208	molecular_function	AMP binding
P	0016779	molecular_function	nucleotidyltransferase activity
P	0042802	molecular_function	identical protein binding
P	0051289	biological_process	protein homotetramerization

Functional Information from PROSITE/UniProt

site_id	PS00808
Number of Residues	20
Details	ADP_GLC_PYROPHOSPH_1 ADP-glucose pyrophosphorylase signature 1. AGGrGTrLkdLTnkrAkPAV

Chain	Residue	Details
A	ALA26-VAL45

site_id	PS00809
Number of Residues	9
Details	ADP_GLC_PYROPHOSPH_2 ADP-glucose pyrophosphorylase signature 2. WYrGTADAV

Chain	Residue	Details
A	TRP113-VAL121

site_id	PS00810
Number of Residues	11
Details	ADP_GLC_PYROPHOSPH_3 ADP-glucose pyrophosphorylase signature 3. ASMGIYVFdaD

Chain	Residue	Details
A	ALA211-ASP221

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	16
Details	BINDING: BINDING => ECO:0000269\|PubMed:27545622, ECO:0000305\|PubMed:2162151

Chain	Residue	Details
A	LYS39
J	LYS39
K	LYS39
L	LYS39
M	LYS39
N	LYS39
O	LYS39
P	LYS39
B	LYS39
C	LYS39
D	LYS39
E	LYS39
F	LYS39
G	LYS39
H	LYS39
I	LYS39

site_id	SWS_FT_FI2
Number of Residues	128
Details	BINDING: BINDING => ECO:0000269\|PubMed:27545622

Chain	Residue	Details
A	ARG40
B	HIS46
M	ARG130
M	GLU370
M	ARG386
M	ARG419
M	GLN429
N	ARG40
N	HIS46
N	ARG52
N	ARG130
N	GLU370
B	ARG52
N	ARG386
N	ARG419
N	GLN429
O	ARG40
O	HIS46
O	ARG52
O	ARG130
O	GLU370
O	ARG386
O	ARG419
B	ARG130
O	GLN429
P	ARG40
P	HIS46
P	ARG52
P	ARG130
P	GLU370
P	ARG386
P	ARG419
P	GLN429
B	GLU370
B	ARG386
B	ARG419
B	GLN429
C	ARG40
C	HIS46
C	ARG52
A	HIS46
C	ARG130
C	GLU370
C	ARG386
C	ARG419
C	GLN429
D	ARG40
D	HIS46
D	ARG52
D	ARG130
D	GLU370
A	ARG52
D	ARG386
D	ARG419
D	GLN429
E	ARG40
E	HIS46
E	ARG52
E	ARG130
E	GLU370
E	ARG386
E	ARG419
A	ARG130
E	GLN429
F	ARG40
F	HIS46
F	ARG52
F	ARG130
F	GLU370
F	ARG386
F	ARG419
F	GLN429
G	ARG40
A	GLU370
G	HIS46
G	ARG52
G	ARG130
G	GLU370
G	ARG386
G	ARG419
G	GLN429
H	ARG40
H	HIS46
H	ARG52
A	ARG386
H	ARG130
H	GLU370
H	ARG386
H	ARG419
H	GLN429
I	ARG40
I	HIS46
I	ARG52
I	ARG130
I	GLU370
A	ARG419
I	ARG386
I	ARG419
I	GLN429
J	ARG40
J	HIS46
J	ARG52
J	ARG130
J	GLU370
J	ARG386
J	ARG419
A	GLN429
J	GLN429
K	ARG40
K	HIS46
K	ARG52
K	ARG130
K	GLU370
K	ARG386
K	ARG419
K	GLN429
L	ARG40
B	ARG40
L	HIS46
L	ARG52
L	ARG130
L	GLU370
L	ARG386
L	ARG419
L	GLN429
M	ARG40
M	HIS46
M	ARG52

site_id	SWS_FT_FI3
Number of Residues	16
Details	BINDING: BINDING => ECO:0000305\|PubMed:2844780

Chain	Residue	Details
A	TYR114
J	TYR114
K	TYR114
L	TYR114
M	TYR114
N	TYR114
O	TYR114
P	TYR114
B	TYR114
C	TYR114
D	TYR114
E	TYR114
F	TYR114
G	TYR114
H	TYR114
I	TYR114

site_id	SWS_FT_FI4
Number of Residues	32
Details	BINDING: BINDING => ECO:0000305\|PubMed:27545622

Chain	Residue	Details
A	GLY179
E	SER212
F	GLY179
F	SER212
G	GLY179
G	SER212
H	GLY179
H	SER212
I	GLY179
I	SER212
J	GLY179
A	SER212
J	SER212
K	GLY179
K	SER212
L	GLY179
L	SER212
M	GLY179
M	SER212
N	GLY179
N	SER212
O	GLY179
B	GLY179
O	SER212
P	GLY179
P	SER212
B	SER212
C	GLY179
C	SER212
D	GLY179
D	SER212
E	GLY179

site_id	SWS_FT_FI5
Number of Residues	16
Details	BINDING: BINDING => ECO:0000305\|PubMed:1648099, ECO:0000305\|PubMed:27545622

Chain	Residue	Details
A	GLU194
J	GLU194
K	GLU194
L	GLU194
M	GLU194
N	GLU194
O	GLU194
P	GLU194
B	GLU194
C	GLU194
D	GLU194
E	GLU194
F	GLU194
G	GLU194
H	GLU194
I	GLU194

site_id	SWS_FT_FI6
Number of Residues	32
Details	SITE: Could play a key role in the communication between the regulatory and the substrate sites => ECO:0000305\|PubMed:21741429

Chain	Residue	Details
A	GLN74
E	TRP113
F	GLN74
F	TRP113
G	GLN74
G	TRP113
H	GLN74
H	TRP113
I	GLN74
I	TRP113
J	GLN74
A	TRP113
J	TRP113
K	GLN74
K	TRP113
L	GLN74
L	TRP113
M	GLN74
M	TRP113
N	GLN74
N	TRP113
O	GLN74
B	GLN74
O	TRP113
P	GLN74
P	TRP113
B	TRP113
C	GLN74
C	TRP113
D	GLN74
D	TRP113
E	GLN74

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