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	0005978	biological_process	glycogen biosynthetic process
A	0008878	molecular_function	glucose-1-phosphate adenylyltransferase activity
A	0009058	biological_process	biosynthetic process
A	0009250	biological_process	glucan 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	0005978	biological_process	glycogen biosynthetic process
B	0008878	molecular_function	glucose-1-phosphate adenylyltransferase activity
B	0009058	biological_process	biosynthetic process
B	0009250	biological_process	glucan 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	0005978	biological_process	glycogen biosynthetic process
C	0008878	molecular_function	glucose-1-phosphate adenylyltransferase activity
C	0009058	biological_process	biosynthetic process
C	0009250	biological_process	glucan 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	0005978	biological_process	glycogen biosynthetic process
D	0008878	molecular_function	glucose-1-phosphate adenylyltransferase activity
D	0009058	biological_process	biosynthetic process
D	0009250	biological_process	glucan 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	0005978	biological_process	glycogen biosynthetic process
E	0008878	molecular_function	glucose-1-phosphate adenylyltransferase activity
E	0009058	biological_process	biosynthetic process
E	0009250	biological_process	glucan 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	0005978	biological_process	glycogen biosynthetic process
F	0008878	molecular_function	glucose-1-phosphate adenylyltransferase activity
F	0009058	biological_process	biosynthetic process
F	0009250	biological_process	glucan 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	0005978	biological_process	glycogen biosynthetic process
G	0008878	molecular_function	glucose-1-phosphate adenylyltransferase activity
G	0009058	biological_process	biosynthetic process
G	0009250	biological_process	glucan 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	0005978	biological_process	glycogen biosynthetic process
H	0008878	molecular_function	glucose-1-phosphate adenylyltransferase activity
H	0009058	biological_process	biosynthetic process
H	0009250	biological_process	glucan 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	76
Details	Binding site: {"evidences":[{"source":"PubMed","id":"27545622","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	16
Details	Binding site: {"evidences":[{"source":"PubMed","id":"27545622","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	8
Details	Binding site: {"evidences":[{"source":"PubMed","id":"1648099","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"27545622","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	8
Details	Site: {"description":"Could play a key role in the communication between the regulatory and the substrate sites","evidences":[{"source":"PubMed","id":"21741429","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"27545622","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"2162151","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	1
Details	Binding site: {"evidences":[{"source":"PubMed","id":"2844780","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

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