6YBU

Crystal structure of a native BcsE (349-523) RQ complex with c-di-GMP and ATP bound

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0005524	molecular_function	ATP binding
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0009898	cellular_component	cytoplasmic side of plasma membrane
A	0016887	molecular_function	ATP hydrolysis activity
A	0051782	biological_process	negative regulation of cell division
B	0000166	molecular_function	nucleotide binding
B	0005524	molecular_function	ATP binding
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0009898	cellular_component	cytoplasmic side of plasma membrane
B	0016887	molecular_function	ATP hydrolysis activity
B	0051782	biological_process	negative regulation of cell division
C	0030244	biological_process	cellulose biosynthetic process
C	0090540	biological_process	bacterial cellulose biosynthetic process
D	0030244	biological_process	cellulose biosynthetic process
D	0090540	biological_process	bacterial cellulose biosynthetic process
E	0035438	molecular_function	cyclic-di-GMP binding
F	0035438	molecular_function	cyclic-di-GMP binding
G	0000166	molecular_function	nucleotide binding
G	0005524	molecular_function	ATP binding
G	0005737	cellular_component	cytoplasm
G	0005829	cellular_component	cytosol
G	0009898	cellular_component	cytoplasmic side of plasma membrane
G	0016887	molecular_function	ATP hydrolysis activity
G	0051782	biological_process	negative regulation of cell division
H	0000166	molecular_function	nucleotide binding
H	0005524	molecular_function	ATP binding
H	0005737	cellular_component	cytoplasm
H	0005829	cellular_component	cytosol
H	0009898	cellular_component	cytoplasmic side of plasma membrane
H	0016887	molecular_function	ATP hydrolysis activity
H	0051782	biological_process	negative regulation of cell division
I	0030244	biological_process	cellulose biosynthetic process
I	0090540	biological_process	bacterial cellulose biosynthetic process
J	0030244	biological_process	cellulose biosynthetic process
J	0090540	biological_process	bacterial cellulose biosynthetic process
K	0035438	molecular_function	cyclic-di-GMP binding
L	0035438	molecular_function	cyclic-di-GMP binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	25
Details	binding site for residue ATP A 301

Chain	Residue
A	GLY11
A	HIS200
A	ARG201
A	ASP202
A	MET205
A	ALA206
A	MG302
A	HOH413
A	HOH414
A	HOH420
A	HOH424
A	GLY12
A	HOH429
B	ARG10
B	ASP150
B	ALA151
B	ASN152
B	ARG156
A	VAL13
A	GLY14
A	THR15
A	THR16
A	THR17
A	ASN171
A	ASN172

---

site_id	AC2
Number of Residues	5
Details	binding site for residue MG A 302

Chain	Residue
A	THR16
A	ATP301
A	HOH413
A	HOH424
A	HOH429

---

site_id	AC3
Number of Residues	24
Details	binding site for residue ATP B 301

Chain	Residue
A	ARG10
A	ASP150
A	ALA151
A	ASN152
A	ARG156
B	GLY11
B	GLY12
B	VAL13
B	GLY14
B	THR15
B	THR16
B	THR17
B	LEU43
B	ASN171
B	ASN172
B	HIS200
B	ARG201
B	ASP202
B	MET205
B	ALA206
B	MG302
B	HOH406
B	HOH410
B	HOH412

---

site_id	AC4
Number of Residues	5
Details	binding site for residue MG B 302

Chain	Residue
B	THR16
B	ATP301
B	HOH410
B	HOH413
B	HOH432

---

site_id	AC5
Number of Residues	8
Details	binding site for residue C2E E 601

Chain	Residue
E	ASN414
E	ARG415
E	THR416
E	HIS445
E	C2E602
I	ARG51
K	ARG503
K	HIS504

---

site_id	AC6
Number of Residues	10
Details	binding site for residue C2E E 602

Chain	Residue
E	ARG415
E	ASP418
E	SER432
E	CYS434
E	ASP438
E	THR441
E	ALA442
E	HIS445
E	C2E601
K	ARG503

---

site_id	AC7
Number of Residues	12
Details	binding site for residue C2E F 601

Chain	Residue
F	ARG415
F	ASP418
F	SER432
F	CYS434
F	ASP438
F	THR441
F	ALA442
F	HIS445
F	C2E602
F	HOH704
F	HOH709
L	ARG503

---

site_id	AC8
Number of Residues	25
Details	binding site for residue ATP G 301

Chain	Residue
G	ARG201
G	ASP202
G	MET205
G	ALA206
G	MG302
G	HOH403
G	HOH410
G	HOH411
G	HOH423
G	HOH426
H	ARG10
H	ASP150
H	ALA151
H	ASN152
H	ARG156
G	GLY11
G	GLY12
G	VAL13
G	GLY14
G	THR15
G	THR16
G	THR17
G	ASN171
G	ASN172
G	HIS200

---

site_id	AC9
Number of Residues	5
Details	binding site for residue MG G 302

Chain	Residue
G	THR16
G	ATP301
G	HOH423
G	HOH426
G	HOH429

---

site_id	AD1
Number of Residues	24
Details	binding site for residue ATP H 301

Chain	Residue
G	ARG10
G	ASP150
G	ALA151
G	ASN152
G	ARG156
H	GLY11
H	GLY12
H	VAL13
H	GLY14
H	THR15
H	THR16
H	THR17
H	ASN171
H	ASN172
H	HIS200
H	ARG201
H	ASP202
H	MET205
H	ALA206
H	MG302
H	HOH403
H	HOH405
H	HOH409
H	HOH425

---

site_id	AD2
Number of Residues	5
Details	binding site for residue MG H 302

Chain	Residue
H	THR16
H	ATP301
H	HOH422
H	HOH425
H	HOH428

---

site_id	AD3
Number of Residues	12
Details	binding site for residue C2E K 602

Chain	Residue
E	ARG503
K	ARG415
K	ASP418
K	SER432
K	CYS434
K	ASP438
K	THR441
K	ALA442
K	HIS445
K	C2E601
K	HOH702
K	HOH708

---

site_id	AD4
Number of Residues	9
Details	binding site for residue C2E L 601

Chain	Residue
B	ARG219
D	ARG51
F	ARG503
F	HIS504
L	ASN414
L	ARG415
L	THR416
L	HIS445
L	C2E602

---

site_id	AD5
Number of Residues	14
Details	binding site for residue C2E L 602

Chain	Residue
F	ARG503
L	ARG415
L	ASP418
L	LEU431
L	SER432
L	CYS434
L	ASP438
L	THR441
L	ALA442
L	HIS445
L	C2E601
L	HOH708
L	HOH709
L	HOH710

---

site_id	AD6
Number of Residues	33
Details	binding site for Di-peptide C2E F 602 and ARG L 503

Chain	Residue
F	ASN414
F	ARG415
F	ARG415
F	THR416
F	HIS445
F	HIS500
F	ASP501
F	GLY502
F	HIS504
F	C2E601
F	C2E601
H	ARG219
J	ARG51
L	ARG415
L	ARG415
L	ASP418
L	LEU431
L	SER432
L	CYS434
L	ASP438
L	THR441
L	ALA442
L	HIS445
L	HIS500
L	ASP501
L	GLY502
L	HIS504
L	HIS504
L	C2E601
L	C2E601
L	HOH708
L	HOH709
L	HOH710

---

site_id	AD7
Number of Residues	28
Details	binding site for Di-peptide C2E K 601 and ARG E 503

Chain	Residue
A	ARG219
C	ARG51
E	ASN414
E	ARG415
E	ARG415
E	THR416
E	HIS445
E	HIS500
E	ASP501
E	GLY502
E	HIS504
E	HIS504
E	C2E602
E	C2E602
I	ARG51
K	ASN414
K	ARG415
K	ARG415
K	THR416
K	HIS445
K	HIS500
K	ASP501
K	GLY502
K	HIS504
K	HIS504
K	C2E602
K	C2E602
K	HOH709

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	BINDING: BINDING => ECO:0000255

Chain	Residue	Details
A	VAL9
B	VAL9
G	VAL9
H	VAL9

---