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Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

8EFR

CryoEM of the soluble OPA1 interfaces with GDP-AlFx bound from the helical assembly on a lipid membrane

This is a non-PDB format compatible entry.

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
Q	0003924	molecular_function	GTPase activity
Q	0005525	molecular_function	GTP binding
R	0003924	molecular_function	GTPase activity
R	0005525	molecular_function	GTP binding

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	180
Details	INTRAMEM: INTRAMEM => ECO:0000269\|PubMed:37612504, ECO:0000269\|PubMed:37612506

Chain	Residue	Details
A	TRP771-ARG781
N	TRP771-ARG781
G	TRP771-ARG781
O	TRP771-ARG781
H	TRP771-ARG781
P	TRP771-ARG781
I	TRP771-ARG781
Q	TRP771-ARG781
J	TRP771-ARG781
R	TRP771-ARG781
B	TRP771-ARG781
C	TRP771-ARG781
K	TRP771-ARG781
D	TRP771-ARG781
L	TRP771-ARG781
E	TRP771-ARG781
M	TRP771-ARG781
F	TRP771-ARG781

site_id	SWS_FT_FI2
Number of Residues	3204
Details	TOPO_DOM: Mitochondrial intermembrane => ECO:0000305\|PubMed:37612504, ECO:0000305\|PubMed:37612506

Chain	Residue	Details
A	THR782-LYS960
N	THR782-LYS960
G	THR782-LYS960
O	THR782-LYS960
H	THR782-LYS960
P	THR782-LYS960
I	THR782-LYS960
Q	THR782-LYS960
J	THR782-LYS960
R	THR782-LYS960
B	THR782-LYS960
C	THR782-LYS960
K	THR782-LYS960
D	THR782-LYS960
L	THR782-LYS960
E	THR782-LYS960
M	THR782-LYS960
F	THR782-LYS960

site_id	SWS_FT_FI3
Number of Residues	180
Details	BINDING: BINDING => ECO:0000305\|PubMed:32379273, ECO:0007744\|PDB:6JTG

Chain	Residue	Details
A	SER298
A	THR503
N	THR503
G	SER298
G	GLY300
G	LYS301
G	THR302
G	GLY317
G	THR323
G	ASP398
G	LYS468
G	ASP470
B	SER298
G	THR503
O	SER298
O	GLY300
O	LYS301
O	THR302
O	GLY317
O	THR323
O	ASP398
O	LYS468
O	ASP470
B	GLY300
O	THR503
H	SER298
H	GLY300
H	LYS301
H	THR302
H	GLY317
H	THR323
H	ASP398
H	LYS468
H	ASP470
B	LYS301
H	THR503
P	SER298
P	GLY300
P	LYS301
P	THR302
P	GLY317
P	THR323
P	ASP398
P	LYS468
P	ASP470
B	THR302
P	THR503
I	SER298
I	GLY300
I	LYS301
I	THR302
I	GLY317
I	THR323
I	ASP398
I	LYS468
I	ASP470
B	GLY317
I	THR503
Q	SER298
Q	GLY300
Q	LYS301
Q	THR302
Q	GLY317
Q	THR323
Q	ASP398
Q	LYS468
Q	ASP470
B	THR323
Q	THR503
J	SER298
J	GLY300
J	LYS301
J	THR302
J	GLY317
J	THR323
J	ASP398
J	LYS468
J	ASP470
B	ASP398
J	THR503
R	SER298
R	GLY300
R	LYS301
R	THR302
R	GLY317
R	THR323
R	ASP398
R	LYS468
R	ASP470
B	LYS468
R	THR503
B	ASP470
A	GLY300
B	THR503
C	SER298
C	GLY300
C	LYS301
C	THR302
C	GLY317
C	THR323
C	ASP398
C	LYS468
C	ASP470
A	LYS301
C	THR503
K	SER298
K	GLY300
K	LYS301
K	THR302
K	GLY317
K	THR323
K	ASP398
K	LYS468
K	ASP470
A	THR302
K	THR503
D	SER298
D	GLY300
D	LYS301
D	THR302
D	GLY317
D	THR323
D	ASP398
D	LYS468
D	ASP470
A	GLY317
D	THR503
L	SER298
L	GLY300
L	LYS301
L	THR302
L	GLY317
L	THR323
L	ASP398
L	LYS468
L	ASP470
A	THR323
L	THR503
E	SER298
E	GLY300
E	LYS301
E	THR302
E	GLY317
E	THR323
E	ASP398
E	LYS468
E	ASP470
A	ASP398
E	THR503
M	SER298
M	GLY300
M	LYS301
M	THR302
M	GLY317
M	THR323
M	ASP398
M	LYS468
M	ASP470
A	LYS468
M	THR503
F	SER298
F	GLY300
F	LYS301
F	THR302
F	GLY317
F	THR323
F	ASP398
F	LYS468
F	ASP470
A	ASP470
F	THR503
N	SER298
N	GLY300
N	LYS301
N	THR302
N	GLY317
N	THR323
N	ASP398
N	LYS468
N	ASP470

site_id	SWS_FT_FI4
Number of Residues	18
Details	BINDING: BINDING => ECO:0000305\|PubMed:32379273, ECO:0000305\|PubMed:37612506, ECO:0007744\|PDB:6JTG, ECO:0007744\|PDB:8EEW

Chain	Residue	Details
A	SER303
N	SER303
G	SER303
O	SER303
H	SER303
P	SER303
I	SER303
Q	SER303
J	SER303
R	SER303
B	SER303
C	SER303
K	SER303
D	SER303
L	SER303
E	SER303
M	SER303
F	SER303

site_id	SWS_FT_FI5
Number of Residues	36
Details	BINDING: BINDING => ECO:0000305\|PubMed:37612506, ECO:0007744\|PDB:8EEW

Chain	Residue	Details
A	GLY506
D	ASN507
L	GLY506
L	ASN507
E	GLY506
E	ASN507
M	GLY506
M	ASN507
F	GLY506
F	ASN507
N	GLY506
A	ASN507
N	ASN507
G	GLY506
G	ASN507
O	GLY506
O	ASN507
H	GLY506
H	ASN507
P	GLY506
P	ASN507
I	GLY506
B	GLY506
I	ASN507
Q	GLY506
Q	ASN507
J	GLY506
J	ASN507
R	GLY506
R	ASN507
B	ASN507
C	GLY506
C	ASN507
K	GLY506
K	ASN507
D	GLY506

site_id	SWS_FT_FI6
Number of Residues	18
Details	MOD_RES: N6-acetyllysine => ECO:0007744\|PubMed:19608861

Chain	Residue	Details
A	LYS228
N	LYS228
G	LYS228
O	LYS228
H	LYS228
P	LYS228
I	LYS228
Q	LYS228
J	LYS228
R	LYS228
B	LYS228
C	LYS228
K	LYS228
D	LYS228
L	LYS228
E	LYS228
M	LYS228
F	LYS228

227344

PDB entries from 2024-11-13

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