6RZV

Structure of s-Mgm1 decorating the inner surface of tubulated lipid membranes

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003924	molecular_function	GTPase activity
A	0005525	molecular_function	GTP binding
B	0003924	molecular_function	GTPase activity
B	0005525	molecular_function	GTP binding
C	0003924	molecular_function	GTPase activity
C	0005525	molecular_function	GTP binding
D	0003924	molecular_function	GTPase activity
D	0005525	molecular_function	GTP binding
E	0003924	molecular_function	GTPase activity
E	0005525	molecular_function	GTP binding
F	0003924	molecular_function	GTPase activity
F	0005525	molecular_function	GTP binding
G	0003924	molecular_function	GTPase activity
G	0005525	molecular_function	GTP binding
H	0003924	molecular_function	GTPase activity
H	0005525	molecular_function	GTP binding
I	0003924	molecular_function	GTPase activity
I	0005525	molecular_function	GTP binding
J	0003924	molecular_function	GTPase activity
J	0005525	molecular_function	GTP binding
K	0003924	molecular_function	GTPase activity
K	0005525	molecular_function	GTP binding
L	0003924	molecular_function	GTPase activity
L	0005525	molecular_function	GTP binding
M	0003924	molecular_function	GTPase activity
M	0005525	molecular_function	GTP binding
N	0003924	molecular_function	GTPase activity
N	0005525	molecular_function	GTP binding
O	0003924	molecular_function	GTPase activity
O	0005525	molecular_function	GTP binding
P	0003924	molecular_function	GTPase activity
P	0005525	molecular_function	GTP binding

Functional Information from PROSITE/UniProt

site_id	PS00410
Number of Residues	10
Details	G_DYNAMIN_1 Dynamin-type guanine nucleotide-binding (G) domain signature. LPKGSNMITR

Chain	Residue	Details
A	LEU278-ARG287

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	176
Details	BINDING: BINDING => ECO:0000250|UniProtKB:O60313

Chain	Residue	Details
A	SER262
A	ASP430
J	SER262
J	GLY264
J	LYS265
J	SER266
J	SER267
J	GLY281
J	THR286
J	ASP359
J	LYS428
J	ASP430
A	SER457
J	SER457
K	SER262
K	GLY264
K	LYS265
K	SER266
K	SER267
K	GLY281
K	THR286
K	ASP359
K	LYS428
B	SER262
K	ASP430
K	SER457
L	SER262
L	GLY264
L	LYS265
L	SER266
L	SER267
L	GLY281
L	THR286
L	ASP359
B	GLY264
L	LYS428
L	ASP430
L	SER457
M	SER262
M	GLY264
M	LYS265
M	SER266
M	SER267
M	GLY281
M	THR286
B	LYS265
M	ASP359
M	LYS428
M	ASP430
M	SER457
N	SER262
N	GLY264
N	LYS265
N	SER266
N	SER267
N	GLY281
B	SER266
N	THR286
N	ASP359
N	LYS428
N	ASP430
N	SER457
O	SER262
O	GLY264
O	LYS265
O	SER266
O	SER267
B	SER267
O	GLY281
O	THR286
O	ASP359
O	LYS428
O	ASP430
O	SER457
P	SER262
P	GLY264
P	LYS265
P	SER266
B	GLY281
P	SER267
P	GLY281
P	THR286
P	ASP359
P	LYS428
P	ASP430
P	SER457
B	THR286
B	ASP359
A	GLY264
B	LYS428
B	ASP430
B	SER457
C	SER262
C	GLY264
C	LYS265
C	SER266
C	SER267
C	GLY281
C	THR286
A	LYS265
C	ASP359
C	LYS428
C	ASP430
C	SER457
D	SER262
D	GLY264
D	LYS265
D	SER266
D	SER267
D	GLY281
A	SER266
D	THR286
D	ASP359
D	LYS428
D	ASP430
D	SER457
E	SER262
E	GLY264
E	LYS265
E	SER266
E	SER267
A	SER267
E	GLY281
E	THR286
E	ASP359
E	LYS428
E	ASP430
E	SER457
F	SER262
F	GLY264
F	LYS265
F	SER266
A	GLY281
F	SER267
F	GLY281
F	THR286
F	ASP359
F	LYS428
F	ASP430
F	SER457
G	SER262
G	GLY264
G	LYS265
A	THR286
G	SER266
G	SER267
G	GLY281
G	THR286
G	ASP359
G	LYS428
G	ASP430
G	SER457
H	SER262
H	GLY264
A	ASP359
H	LYS265
H	SER266
H	SER267
H	GLY281
H	THR286
H	ASP359
H	LYS428
H	ASP430
H	SER457
I	SER262
A	LYS428
I	GLY264
I	LYS265
I	SER266
I	SER267
I	GLY281
I	THR286
I	ASP359
I	LYS428
I	ASP430
I	SER457

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