8RB8

Cryo-EM structure of the NADH:ferredoxin oxidoreductase RNF from Azotobacter vinelandii, purified with 2-ME/TCEP, NADH added

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005886	cellular_component	plasma membrane
A	0016020	cellular_component	membrane
A	0022900	biological_process	electron transport chain
B	0005886	cellular_component	plasma membrane
B	0009055	molecular_function	electron transfer activity
B	0022900	biological_process	electron transport chain
B	0051536	molecular_function	iron-sulfur cluster binding
B	0051539	molecular_function	4 iron, 4 sulfur cluster binding
C	0005886	cellular_component	plasma membrane
C	0009055	molecular_function	electron transfer activity
C	0016020	cellular_component	membrane
C	0022900	biological_process	electron transport chain
C	0051539	molecular_function	4 iron, 4 sulfur cluster binding
D	0005886	cellular_component	plasma membrane
D	0016020	cellular_component	membrane
D	0022900	biological_process	electron transport chain
D	0055085	biological_process	transmembrane transport
E	0005886	cellular_component	plasma membrane
E	0016020	cellular_component	membrane
E	0022900	biological_process	electron transport chain
G	0005886	cellular_component	plasma membrane
G	0009055	molecular_function	electron transfer activity
G	0010181	molecular_function	FMN binding
G	0016020	cellular_component	membrane
G	0022900	biological_process	electron transport chain

Functional Information from PROSITE/UniProt

site_id	PS00198
Number of Residues	12
Details	4FE4S_FER_1 4Fe-4S ferredoxin-type iron-sulfur binding region signature. CiGCTrCYrACP

Chain	Residue	Details
B	CYS109-PRO120
B	CYS139-PRO150
C	CYS370-PRO381
C	CYS409-PRO420

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI12
Number of Residues	120
Details	Transmembrane: {"description":"Helical","evidences":[{"source":"HAMAP-Rule","id":"MF_00478","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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