6SI8

Escherichia coli AGPase in complex with AMP.

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0000287	molecular_function	magnesium ion binding
A	0003824	molecular_function	catalytic activity
A	0005524	molecular_function	ATP binding
A	0005977	biological_process	glycogen metabolic process
A	0005978	biological_process	glycogen biosynthetic process
A	0008152	biological_process	metabolic 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	0016740	molecular_function	transferase activity
A	0016779	molecular_function	nucleotidyltransferase activity
A	0042802	molecular_function	identical protein binding
A	0051289	biological_process	protein homotetramerization
B	0000166	molecular_function	nucleotide binding
B	0000287	molecular_function	magnesium ion binding
B	0003824	molecular_function	catalytic activity
B	0005524	molecular_function	ATP binding
B	0005977	biological_process	glycogen metabolic process
B	0005978	biological_process	glycogen biosynthetic process
B	0008152	biological_process	metabolic 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	0016740	molecular_function	transferase activity
B	0016779	molecular_function	nucleotidyltransferase activity
B	0042802	molecular_function	identical protein binding
B	0051289	biological_process	protein homotetramerization
C	0000166	molecular_function	nucleotide binding
C	0000287	molecular_function	magnesium ion binding
C	0003824	molecular_function	catalytic activity
C	0005524	molecular_function	ATP binding
C	0005977	biological_process	glycogen metabolic process
C	0005978	biological_process	glycogen biosynthetic process
C	0008152	biological_process	metabolic 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	0016740	molecular_function	transferase activity
C	0016779	molecular_function	nucleotidyltransferase activity
C	0042802	molecular_function	identical protein binding
C	0051289	biological_process	protein homotetramerization
D	0000166	molecular_function	nucleotide binding
D	0000287	molecular_function	magnesium ion binding
D	0003824	molecular_function	catalytic activity
D	0005524	molecular_function	ATP binding
D	0005977	biological_process	glycogen metabolic process
D	0005978	biological_process	glycogen biosynthetic process
D	0008152	biological_process	metabolic 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	0016740	molecular_function	transferase activity
D	0016779	molecular_function	nucleotidyltransferase activity
D	0042802	molecular_function	identical protein binding
D	0051289	biological_process	protein homotetramerization

Functional Information from PDB Data

site_id	AC1
Number of Residues	8
Details	binding site for residue AMP A 501

Chain	Residue
A	ARG40
A	HIS46
A	ARG52
A	THR79
A	GLU370
A	ARG386
A	ALA387
C	ARG130

---

site_id	AC2
Number of Residues	10
Details	binding site for residue AMP B 501

Chain	Residue
B	ARG40
B	HIS46
B	ARG52
B	THR79
B	GLU370
B	ARG386
B	ALA387
B	ARG419
D	ARG130
B	LYS39

---

site_id	AC3
Number of Residues	9
Details	binding site for residue AMP D 501

Chain	Residue
B	ARG130
D	ARG40
D	HIS46
D	ARG52
D	THR79
D	GLU370
D	ARG386
D	ALA387
D	ARG419

---

site_id	AC4
Number of Residues	9
Details	binding site for residue AMP C 501

Chain	Residue
A	ARG130
C	ARG40
C	HIS46
C	ARG52
C	THR79
C	GLU370
C	ARG386
C	ALA387
C	ARG419

---

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	4
Details	BINDING: BINDING => ECO:0000269|PubMed:27545622, ECO:0000305|PubMed:2162151

Chain	Residue	Details
A	LYS39
B	LYS39
D	LYS39
C	LYS39

---

site_id	SWS_FT_FI2
Number of Residues	32
Details	BINDING: BINDING => ECO:0000269|PubMed:27545622

Chain	Residue	Details
A	ARG40
B	HIS46
B	ARG52
B	ARG130
B	GLU370
B	ARG386
B	ARG419
B	GLN429
D	ARG40
D	HIS46
D	ARG52
A	HIS46
D	ARG130
D	GLU370
D	ARG386
D	ARG419
D	GLN429
C	ARG40
C	HIS46
C	ARG52
C	ARG130
C	GLU370
A	ARG52
C	ARG386
C	ARG419
C	GLN429
A	ARG130
A	GLU370
A	ARG386
A	ARG419
A	GLN429
B	ARG40

---

site_id	SWS_FT_FI3
Number of Residues	4
Details	BINDING: BINDING => ECO:0000305|PubMed:2844780

Chain	Residue	Details
A	TYR114
B	TYR114
D	TYR114
C	TYR114

---

site_id	SWS_FT_FI4
Number of Residues	8
Details	BINDING: BINDING => ECO:0000305|PubMed:27545622

Chain	Residue	Details
A	GLY179
A	SER212
B	GLY179
B	SER212
D	GLY179
D	SER212
C	GLY179
C	SER212

---

site_id	SWS_FT_FI5
Number of Residues	4
Details	BINDING: BINDING => ECO:0000305|PubMed:1648099, ECO:0000305|PubMed:27545622

Chain	Residue	Details
A	GLU194
B	GLU194
D	GLU194
C	GLU194

---

site_id	SWS_FT_FI6
Number of Residues	8
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
A	TRP113
B	GLN74
B	TRP113
D	GLN74
D	TRP113
C	GLN74
C	TRP113

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