Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6RIQ

MinCD filament from Pseudomonas aeruginosa

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000902	biological_process	cell morphogenesis
A	0051726	biological_process	regulation of cell cycle
A	1901891	biological_process	regulation of cell septum assembly
B	0000902	biological_process	cell morphogenesis
B	0051726	biological_process	regulation of cell cycle
B	1901891	biological_process	regulation of cell septum assembly
C	0005524	molecular_function	ATP binding
C	0005829	cellular_component	cytosol
C	0009898	cellular_component	cytoplasmic side of plasma membrane
C	0016887	molecular_function	ATP hydrolysis activity
C	0032506	biological_process	cytokinetic process
D	0005524	molecular_function	ATP binding
D	0005829	cellular_component	cytosol
D	0009898	cellular_component	cytoplasmic side of plasma membrane
D	0016887	molecular_function	ATP hydrolysis activity
D	0032506	biological_process	cytokinetic process
E	0000902	biological_process	cell morphogenesis
E	0051726	biological_process	regulation of cell cycle
E	1901891	biological_process	regulation of cell septum assembly
F	0000902	biological_process	cell morphogenesis
F	0051726	biological_process	regulation of cell cycle
F	1901891	biological_process	regulation of cell septum assembly
G	0005524	molecular_function	ATP binding
G	0005829	cellular_component	cytosol
G	0009898	cellular_component	cytoplasmic side of plasma membrane
G	0016887	molecular_function	ATP hydrolysis activity
G	0032506	biological_process	cytokinetic process
H	0000902	biological_process	cell morphogenesis
H	0051726	biological_process	regulation of cell cycle
H	1901891	biological_process	regulation of cell septum assembly
I	0000902	biological_process	cell morphogenesis
I	0051726	biological_process	regulation of cell cycle
I	1901891	biological_process	regulation of cell septum assembly
J	0005524	molecular_function	ATP binding
J	0005829	cellular_component	cytosol
J	0009898	cellular_component	cytoplasmic side of plasma membrane
J	0016887	molecular_function	ATP hydrolysis activity
J	0032506	biological_process	cytokinetic process
K	0005524	molecular_function	ATP binding
K	0005829	cellular_component	cytosol
K	0009898	cellular_component	cytoplasmic side of plasma membrane
K	0016887	molecular_function	ATP hydrolysis activity
K	0032506	biological_process	cytokinetic process
L	0000902	biological_process	cell morphogenesis
L	0051726	biological_process	regulation of cell cycle
L	1901891	biological_process	regulation of cell septum assembly
M	0005524	molecular_function	ATP binding
M	0005829	cellular_component	cytosol
M	0009898	cellular_component	cytoplasmic side of plasma membrane
M	0016887	molecular_function	ATP hydrolysis activity
M	0032506	biological_process	cytokinetic process
N	0005524	molecular_function	ATP binding
N	0005829	cellular_component	cytosol
N	0009898	cellular_component	cytoplasmic side of plasma membrane
N	0016887	molecular_function	ATP hydrolysis activity
N	0032506	biological_process	cytokinetic process
O	0000902	biological_process	cell morphogenesis
O	0051726	biological_process	regulation of cell cycle
O	1901891	biological_process	regulation of cell septum assembly
P	0000902	biological_process	cell morphogenesis
P	0051726	biological_process	regulation of cell cycle
P	1901891	biological_process	regulation of cell septum assembly
Q	0005524	molecular_function	ATP binding
Q	0005829	cellular_component	cytosol
Q	0009898	cellular_component	cytoplasmic side of plasma membrane
Q	0016887	molecular_function	ATP hydrolysis activity
Q	0032506	biological_process	cytokinetic process
R	0005524	molecular_function	ATP binding
R	0005829	cellular_component	cytosol
R	0009898	cellular_component	cytoplasmic side of plasma membrane
R	0016887	molecular_function	ATP hydrolysis activity
R	0032506	biological_process	cytokinetic process
S	0000902	biological_process	cell morphogenesis
S	0051726	biological_process	regulation of cell cycle
S	1901891	biological_process	regulation of cell septum assembly
T	0000902	biological_process	cell morphogenesis
T	0051726	biological_process	regulation of cell cycle
T	1901891	biological_process	regulation of cell septum assembly
U	0005524	molecular_function	ATP binding
U	0005829	cellular_component	cytosol
U	0009898	cellular_component	cytoplasmic side of plasma membrane
U	0016887	molecular_function	ATP hydrolysis activity
U	0032506	biological_process	cytokinetic process
V	0005524	molecular_function	ATP binding
V	0005829	cellular_component	cytosol
V	0009898	cellular_component	cytoplasmic side of plasma membrane
V	0016887	molecular_function	ATP hydrolysis activity
V	0032506	biological_process	cytokinetic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	3
Details	binding site for residue MG C 301

Chain	Residue
C	THR17
C	ASP119
C	ATP302

site_id	AC2
Number of Residues	3
Details	binding site for residue MG D 301

Chain	Residue
D	THR17
D	ASP119
D	ATP302

site_id	AC3
Number of Residues	3
Details	binding site for residue MG G 301

Chain	Residue
G	THR17
G	ASP119
G	ATP302

site_id	AC4
Number of Residues	3
Details	binding site for residue MG J 301

Chain	Residue
J	THR17
J	ASP119
J	ATP302

site_id	AC5
Number of Residues	3
Details	binding site for residue MG K 301

Chain	Residue
K	THR17
K	ASP119
K	ATP302

site_id	AC6
Number of Residues	3
Details	binding site for residue MG M 301

Chain	Residue
M	THR17
M	ASP119
M	ATP302

site_id	AC7
Number of Residues	3
Details	binding site for residue MG N 301

Chain	Residue
N	THR17
N	ASP119
N	ATP302

site_id	AC8
Number of Residues	3
Details	binding site for residue MG Q 301

Chain	Residue
Q	THR17
Q	ASP119
Q	ATP302

site_id	AC9
Number of Residues	3
Details	binding site for residue MG R 301

Chain	Residue
R	THR17
R	ASP119
R	ATP302

site_id	AD1
Number of Residues	3
Details	binding site for residue MG U 301

Chain	Residue
U	THR17
U	ASP119
U	ATP302

site_id	AD2
Number of Residues	3
Details	binding site for residue MG V 301

Chain	Residue
V	THR17
V	ASP119
V	ATP302

site_id	AD3
Number of Residues	23
Details	binding site for Di-peptide ATP C 302 and LYS C 16

Chain	Residue
C	LYS11
C	GLY12
C	GLY13
C	VAL14
C	GLY15
C	THR17
C	THR18
C	THR19
C	SER20
C	ASN45
C	ASP119
C	SER120
C	THR180
C	ARG181
C	ILE210
C	PRO211
C	GLU212
C	SER213
C	VAL216
C	MG301
D	LYS11
D	GLY12
D	GLU145

site_id	AD4
Number of Residues	23
Details	binding site for Di-peptide ATP D 302 and LYS D 16

Chain	Residue
C	LYS11
C	GLY12
C	GLU145
D	LYS11
D	GLY12
D	GLY13
D	VAL14
D	GLY15
D	THR17
D	THR18
D	THR19
D	SER20
D	ASN45
D	ASP119
D	SER120
D	THR180
D	ARG181
D	ILE210
D	PRO211
D	GLU212
D	SER213
D	VAL216
D	MG301

site_id	AD5
Number of Residues	20
Details	binding site for Di-peptide ATP G 302 and LYS G 16

Chain	Residue
G	LYS11
G	GLY12
G	GLY13
G	VAL14
G	GLY15
G	THR17
G	THR18
G	THR19
G	SER20
G	ASN45
G	ASP119
G	SER120
G	THR180
G	ARG181
G	ILE210
G	PRO211
G	GLU212
G	SER213
G	VAL216
G	MG301

site_id	AD6
Number of Residues	23
Details	binding site for Di-peptide ATP J 302 and LYS J 16

Chain	Residue
J	LYS11
J	GLY12
J	GLY13
J	VAL14
J	GLY15
J	THR17
J	THR18
J	THR19
J	SER20
J	ASN45
J	ASP119
J	SER120
J	THR180
J	ARG181
J	ILE210
J	PRO211
J	GLU212
J	SER213
J	VAL216
J	MG301
K	LYS11
K	GLY12
K	GLU145

site_id	AD7
Number of Residues	23
Details	binding site for Di-peptide ATP K 302 and LYS K 16

Chain	Residue
J	LYS11
J	GLY12
J	GLU145
K	LYS11
K	GLY12
K	GLY13
K	VAL14
K	GLY15
K	THR17
K	THR18
K	THR19
K	SER20
K	ASN45
K	ASP119
K	SER120
K	THR180
K	ARG181
K	ILE210
K	PRO211
K	GLU212
K	SER213
K	VAL216
K	MG301

site_id	AD8
Number of Residues	23
Details	binding site for Di-peptide ATP M 302 and LYS M 16

Chain	Residue
M	LYS11
M	GLY12
M	GLY13
M	VAL14
M	GLY15
M	THR17
M	THR18
M	THR19
M	SER20
M	ASN45
M	ASP119
M	SER120
M	THR180
M	ARG181
M	ILE210
M	PRO211
M	GLU212
M	SER213
M	VAL216
M	MG301
N	LYS11
N	GLY12
N	GLU145

site_id	AD9
Number of Residues	23
Details	binding site for Di-peptide ATP N 302 and LYS N 16

Chain	Residue
M	LYS11
M	GLY12
M	GLU145
N	LYS11
N	GLY12
N	GLY13
N	VAL14
N	GLY15
N	THR17
N	THR18
N	THR19
N	SER20
N	ASN45
N	ASP119
N	SER120
N	THR180
N	ARG181
N	ILE210
N	PRO211
N	GLU212
N	SER213
N	VAL216
N	MG301

site_id	AE1
Number of Residues	23
Details	binding site for Di-peptide ATP Q 302 and LYS Q 16

Chain	Residue
Q	LYS11
Q	GLY12
Q	GLY13
Q	VAL14
Q	GLY15
Q	THR17
Q	THR18
Q	THR19
Q	SER20
Q	ASN45
Q	ASP119
Q	SER120
Q	THR180
Q	ARG181
Q	ILE210
Q	PRO211
Q	GLU212
Q	SER213
Q	VAL216
Q	MG301
R	LYS11
R	GLY12
R	GLU145

site_id	AE2
Number of Residues	23
Details	binding site for Di-peptide ATP R 302 and LYS R 16

Chain	Residue
Q	LYS11
Q	GLY12
Q	GLU145
R	LYS11
R	GLY12
R	GLY13
R	VAL14
R	GLY15
R	THR17
R	THR18
R	THR19
R	SER20
R	ASN45
R	ASP119
R	SER120
R	THR180
R	ARG181
R	ILE210
R	PRO211
R	GLU212
R	SER213
R	VAL216
R	MG301

site_id	AE3
Number of Residues	23
Details	binding site for Di-peptide ATP U 302 and LYS U 16

Chain	Residue
U	LYS11
U	GLY12
U	GLY13
U	VAL14
U	GLY15
U	THR17
U	THR18
U	THR19
U	SER20
U	ASN45
U	ASP119
U	SER120
U	THR180
U	ARG181
U	ILE210
U	PRO211
U	GLU212
U	SER213
U	VAL216
U	MG301
V	LYS11
V	GLY12
V	GLU145

site_id	AE4
Number of Residues	23
Details	binding site for Di-peptide ATP V 302 and LYS V 16

Chain	Residue
U	LYS11
U	GLY12
U	GLU145
V	LYS11
V	GLY12
V	GLY13
V	VAL14
V	GLY15
V	THR17
V	THR18
V	THR19
V	SER20
V	ASN45
V	ASP119
V	SER120
V	THR180
V	ARG181
V	ILE210
V	PRO211
V	GLU212
V	SER213
V	VAL216
V	MG301

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)