Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6V9A

Agrobacterium tumefaciens ADP-Glucose pyrophosphorylase-S72D

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005978	biological_process	glycogen biosynthetic process
A	0008878	molecular_function	glucose-1-phosphate adenylyltransferase activity
A	0009058	biological_process	biosynthetic process
B	0005978	biological_process	glycogen biosynthetic process
B	0008878	molecular_function	glucose-1-phosphate adenylyltransferase activity
B	0009058	biological_process	biosynthetic process
C	0005978	biological_process	glycogen biosynthetic process
C	0008878	molecular_function	glucose-1-phosphate adenylyltransferase activity
C	0009058	biological_process	biosynthetic process
D	0005978	biological_process	glycogen biosynthetic process
D	0008878	molecular_function	glucose-1-phosphate adenylyltransferase activity
D	0009058	biological_process	biosynthetic process
E	0005978	biological_process	glycogen biosynthetic process
E	0008878	molecular_function	glucose-1-phosphate adenylyltransferase activity
E	0009058	biological_process	biosynthetic process
F	0005978	biological_process	glycogen biosynthetic process
F	0008878	molecular_function	glucose-1-phosphate adenylyltransferase activity
F	0009058	biological_process	biosynthetic process
G	0005978	biological_process	glycogen biosynthetic process
G	0008878	molecular_function	glucose-1-phosphate adenylyltransferase activity
G	0009058	biological_process	biosynthetic process
H	0005978	biological_process	glycogen biosynthetic process
H	0008878	molecular_function	glucose-1-phosphate adenylyltransferase activity
H	0009058	biological_process	biosynthetic process
I	0005978	biological_process	glycogen biosynthetic process
I	0008878	molecular_function	glucose-1-phosphate adenylyltransferase activity
I	0009058	biological_process	biosynthetic process
J	0005978	biological_process	glycogen biosynthetic process
J	0008878	molecular_function	glucose-1-phosphate adenylyltransferase activity
J	0009058	biological_process	biosynthetic process
K	0005978	biological_process	glycogen biosynthetic process
K	0008878	molecular_function	glucose-1-phosphate adenylyltransferase activity
K	0009058	biological_process	biosynthetic process
L	0005978	biological_process	glycogen biosynthetic process
L	0008878	molecular_function	glucose-1-phosphate adenylyltransferase activity
L	0009058	biological_process	biosynthetic process
M	0005978	biological_process	glycogen biosynthetic process
M	0008878	molecular_function	glucose-1-phosphate adenylyltransferase activity
M	0009058	biological_process	biosynthetic process
N	0005978	biological_process	glycogen biosynthetic process
N	0008878	molecular_function	glucose-1-phosphate adenylyltransferase activity
N	0009058	biological_process	biosynthetic process
O	0005978	biological_process	glycogen biosynthetic process
O	0008878	molecular_function	glucose-1-phosphate adenylyltransferase activity
O	0009058	biological_process	biosynthetic process
P	0005978	biological_process	glycogen biosynthetic process
P	0008878	molecular_function	glucose-1-phosphate adenylyltransferase activity
P	0009058	biological_process	biosynthetic process
Q	0005978	biological_process	glycogen biosynthetic process
Q	0008878	molecular_function	glucose-1-phosphate adenylyltransferase activity
Q	0009058	biological_process	biosynthetic process
R	0005978	biological_process	glycogen biosynthetic process
R	0008878	molecular_function	glucose-1-phosphate adenylyltransferase activity
R	0009058	biological_process	biosynthetic process
T	0005978	biological_process	glycogen biosynthetic process
T	0008878	molecular_function	glucose-1-phosphate adenylyltransferase activity
T	0009058	biological_process	biosynthetic process
V	0005978	biological_process	glycogen biosynthetic process
V	0008878	molecular_function	glucose-1-phosphate adenylyltransferase activity
V	0009058	biological_process	biosynthetic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	binding site for residue CIT H 501

Chain	Residue
H	HIS313
H	SER334
H	ASN350
H	SER351
H	ARG368

site_id	AC2
Number of Residues	6
Details	binding site for residue GOL H 502

Chain	Residue
H	HOH640
H	HOH692
H	PRO288
H	ASP291
H	TYR293
H	HOH623

site_id	AC3
Number of Residues	5
Details	binding site for residue CIT A 501

Chain	Residue
A	HIS313
A	SER334
A	ASN350
A	SER351
A	ARG368

site_id	AC4
Number of Residues	6
Details	binding site for residue GOL A 502

Chain	Residue
A	PHE261
A	ASP291
A	TYR293
A	HOH623
A	HOH631
A	HOH683

site_id	AC5
Number of Residues	4
Details	binding site for residue GOL A 503

Chain	Residue
A	ILE332
A	HOH698
B	ASP291
B	HOH620

site_id	AC6
Number of Residues	9
Details	binding site for residue CIT B 501

Chain	Residue
B	HIS313
B	SER334
B	ASN350
B	SER351
B	ARG368
B	HOH610
B	HOH614
B	HOH618
B	HOH647

site_id	AC7
Number of Residues	8
Details	binding site for residue CIT C 501

Chain	Residue
C	HIS313
C	ARG318
C	SER334
C	ASN350
C	SER351
C	ARG368
C	HOH717
C	HOH753

site_id	AC8
Number of Residues	5
Details	binding site for residue GOL C 502

Chain	Residue
C	PRO288
C	ASP291
C	TYR293
C	HOH626
C	HOH645

site_id	AC9
Number of Residues	6
Details	binding site for residue CIT D 501

Chain	Residue
D	HIS313
D	SER334
D	ASN350
D	SER351
D	ARG368
D	HOH755

site_id	AD1
Number of Residues	5
Details	binding site for residue GOL D 502

Chain	Residue
D	ASP291
D	TYR293
D	HOH653
D	HOH659
D	HOH660

site_id	AD2
Number of Residues	6
Details	binding site for residue CIT E 501

Chain	Residue
E	HIS313
E	ARG318
E	SER334
E	ASN350
E	SER351
E	ARG368

site_id	AD3
Number of Residues	5
Details	binding site for residue GOL E 502

Chain	Residue
E	ASP291
E	TYR293
E	HOH606
E	HOH618
E	HOH636

site_id	AD4
Number of Residues	5
Details	binding site for residue CIT F 501

Chain	Residue
F	HIS313
F	SER334
F	ASN350
F	SER351
F	ARG368

site_id	AD5
Number of Residues	6
Details	binding site for residue GOL F 502

Chain	Residue
F	PHE261
F	ASP291
F	TYR293
F	HOH630
F	HOH632
F	HOH634

site_id	AD6
Number of Residues	7
Details	binding site for residue CIT G 501

Chain	Residue
G	HIS313
G	SER334
G	ASN350
G	SER351
G	ARG368
G	HOH630
G	HOH704

site_id	AD7
Number of Residues	5
Details	binding site for residue GOL G 502

Chain	Residue
G	PHE261
G	ASP291
G	TYR293
G	HOH634
G	HOH663

site_id	AD8
Number of Residues	7
Details	binding site for residue CIT I 501

Chain	Residue
I	HOH616
I	HIS313
I	ARG318
I	SER334
I	ASN350
I	SER351
I	ARG368

site_id	AD9
Number of Residues	3
Details	binding site for residue GOL I 502

Chain	Residue
I	ASP291
I	HOH647
I	HOH670

site_id	AE1
Number of Residues	7
Details	binding site for residue CIT J 501

Chain	Residue
J	HIS313
J	SER334
J	ASN350
J	SER351
J	ARG368
J	HOH657
J	HOH712

site_id	AE2
Number of Residues	5
Details	binding site for residue GOL J 502

Chain	Residue
I	LYS310
I	ILE332
J	ASP291
J	HOH608
J	HOH664

site_id	AE3
Number of Residues	6
Details	binding site for residue GOL J 503

Chain	Residue
J	ALA397
J	LYS398
J	PHE400
J	ARG401
J	ARG402
J	HOH690

site_id	AE4
Number of Residues	5
Details	binding site for residue CIT K 501

Chain	Residue
K	HIS313
K	SER334
K	ASN350
K	SER351
K	ARG368

site_id	AE5
Number of Residues	6
Details	binding site for residue GOL K 502

Chain	Residue
K	PHE261
K	ASP291
K	TYR293
K	HOH629
K	HOH652
L	LYS310

site_id	AE6
Number of Residues	10
Details	binding site for residue GOL K 503

Chain	Residue
K	VAL173
K	MET174
K	HIS175
K	VAL176
K	PRO193
K	GLY194
K	ILE195
K	PRO196
K	ALA202
K	LEU203

site_id	AE7
Number of Residues	9
Details	binding site for residue CIT L 501

Chain	Residue
L	HIS313
L	ARG318
L	SER334
L	ASN350
L	SER351
L	ARG368
L	HOH640
L	HOH692
L	HOH706

site_id	AE8
Number of Residues	3
Details	binding site for residue GOL L 502

Chain	Residue
L	ASP291
L	HOH644
L	HOH647

site_id	AE9
Number of Residues	6
Details	binding site for residue CIT M 501

Chain	Residue
M	HIS313
M	SER334
M	ASN350
M	SER351
M	ARG368
M	HOH656

site_id	AF1
Number of Residues	3
Details	binding site for residue GOL M 502

Chain	Residue
M	ASP291
M	HOH621
N	ILE332

site_id	AF2
Number of Residues	6
Details	binding site for residue CIT N 501

Chain	Residue
N	HIS313
N	ARG318
N	SER334
N	ASN350
N	SER351
N	ARG368

site_id	AF3
Number of Residues	6
Details	binding site for residue GOL N 502

Chain	Residue
N	PHE261
N	ASP291
N	TYR293
N	HOH606
N	HOH637
N	HOH666

site_id	AF4
Number of Residues	6
Details	binding site for residue CIT O 501

Chain	Residue
O	HIS313
O	ARG318
O	SER334
O	ASN350
O	SER351
O	ARG368

site_id	AF5
Number of Residues	6
Details	binding site for residue GOL O 502

Chain	Residue
O	ASP291
O	TYR293
O	HOH610
O	HOH623
O	HOH634
O	HOH686

site_id	AF6
Number of Residues	8
Details	binding site for residue CIT P 501

Chain	Residue
P	HIS313
P	SER334
P	ASN350
P	SER351
P	ARG368
P	HOH618
P	HOH681
P	HOH707

site_id	AF7
Number of Residues	6
Details	binding site for residue GOL P 502

Chain	Residue
P	PRO288
P	ASP291
P	TYR293
P	HOH614
P	HOH660
P	HOH704

site_id	AF8
Number of Residues	8
Details	binding site for residue CIT Q 501

Chain	Residue
Q	HIS313
Q	SER334
Q	ASN350
Q	SER351
Q	ARG368
Q	HOH735
Q	HOH744
Q	HOH748

site_id	AF9
Number of Residues	6
Details	binding site for residue GOL Q 502

Chain	Residue
Q	PHE261
Q	ASP291
Q	TYR293
Q	HOH635
Q	HOH643
Q	HOH674

site_id	AG1
Number of Residues	6
Details	binding site for residue CIT R 501

Chain	Residue
R	HIS313
R	SER334
R	ASN350
R	SER351
R	ARG368
R	HOH617

site_id	AG2
Number of Residues	5
Details	binding site for residue GOL R 502

Chain	Residue
R	PHE261
R	ASP291
R	HOH634
R	HOH664
R	HOH670

site_id	AG3
Number of Residues	6
Details	binding site for residue CIT V 501

Chain	Residue
V	HIS313
V	SER334
V	ASN350
V	SER351
V	ARG368
V	HOH708

site_id	AG4
Number of Residues	4
Details	binding site for residue GOL V 502

Chain	Residue
V	ASP291
V	TYR293
V	HOH606
V	HOH682

site_id	AG5
Number of Residues	6
Details	binding site for residue CIT T 501

Chain	Residue
T	HIS313
T	SER334
T	ASN350
T	SER351
T	ARG368
T	HOH723

site_id	AG6
Number of Residues	6
Details	binding site for residue GOL T 502

Chain	Residue
T	PRO288
T	ASP291
T	TYR293
T	HOH619
T	HOH632
T	HOH672

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
H	ALA19-VAL38

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

Chain	Residue	Details
H	TRP106-VAL114

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

Chain	Residue	Details
H	ALA204-LYS214

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	80
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00624","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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