Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

5MNI

Escherichia coli AGPase mutant R130A apo form

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

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
E	ALA26-VAL45

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

Chain	Residue	Details
E	TRP113-VAL121

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

Chain	Residue	Details
E	ALA211-ASP221

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	8
Details	BINDING: BINDING => ECO:0000269\|PubMed:27545622, ECO:0000305\|PubMed:2162151

Chain	Residue	Details
E	LYS39
G	LYS39
H	LYS39
F	LYS39
A	LYS39
B	LYS39
D	LYS39
C	LYS39

site_id	SWS_FT_FI2
Number of Residues	64
Details	BINDING: BINDING => ECO:0000269\|PubMed:27545622

Chain	Residue	Details
E	ARG40
G	HIS46
G	ARG52
G	ALA130
G	GLU370
G	ARG386
G	ARG419
G	GLN429
H	ARG40
H	HIS46
H	ARG52
E	HIS46
H	ALA130
H	GLU370
H	ARG386
H	ARG419
H	GLN429
F	ARG40
F	HIS46
F	ARG52
F	ALA130
F	GLU370
E	ARG52
F	ARG386
F	ARG419
F	GLN429
A	ARG40
A	HIS46
A	ARG52
A	ALA130
A	GLU370
A	ARG386
A	ARG419
E	ALA130
A	GLN429
B	ARG40
B	HIS46
B	ARG52
B	ALA130
B	GLU370
B	ARG386
B	ARG419
B	GLN429
D	ARG40
E	GLU370
D	HIS46
D	ARG52
D	ALA130
D	GLU370
D	ARG386
D	ARG419
D	GLN429
C	ARG40
C	HIS46
C	ARG52
E	ARG386
C	ALA130
C	GLU370
C	ARG386
C	ARG419
C	GLN429
E	ARG419
E	GLN429
G	ARG40

site_id	SWS_FT_FI3
Number of Residues	8
Details	BINDING: BINDING => ECO:0000305\|PubMed:2844780

Chain	Residue	Details
E	TYR114
G	TYR114
H	TYR114
F	TYR114
A	TYR114
B	TYR114
D	TYR114
C	TYR114

site_id	SWS_FT_FI4
Number of Residues	16
Details	BINDING: BINDING => ECO:0000305\|PubMed:27545622

Chain	Residue	Details
E	GLY179
A	SER212
B	GLY179
B	SER212
D	GLY179
D	SER212
C	GLY179
C	SER212
E	SER212
G	GLY179
G	SER212
H	GLY179
H	SER212
F	GLY179
F	SER212
A	GLY179

site_id	SWS_FT_FI5
Number of Residues	8
Details	BINDING: BINDING => ECO:0000305\|PubMed:1648099, ECO:0000305\|PubMed:27545622

Chain	Residue	Details
E	GLU194
G	GLU194
H	GLU194
F	GLU194
A	GLU194
B	GLU194
D	GLU194
C	GLU194

site_id	SWS_FT_FI6
Number of Residues	16
Details	SITE: Could play a key role in the communication between the regulatory and the substrate sites => ECO:0000305\|PubMed:21741429

Chain	Residue	Details
E	GLN74
A	TRP113
B	GLN74
B	TRP113
D	GLN74
D	TRP113
C	GLN74
C	TRP113
E	TRP113
G	GLN74
G	TRP113
H	GLN74
H	TRP113
F	GLN74
F	TRP113
A	GLN74

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