7DEG

Cryo-EM structure of a heme-copper terminal oxidase dimer provides insights into its catalytic mechanism

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004129	molecular_function	cytochrome-c oxidase activity
A	0009060	biological_process	aerobic respiration
A	0016020	cellular_component	membrane
A	0020037	molecular_function	heme binding
A	1902600	biological_process	proton transmembrane transport
B	0004129	molecular_function	cytochrome-c oxidase activity
B	0005507	molecular_function	copper ion binding
B	0016020	cellular_component	membrane
B	0030313	cellular_component	cell envelope
B	1902600	biological_process	proton transmembrane transport
D	0004129	molecular_function	cytochrome-c oxidase activity
D	0009060	biological_process	aerobic respiration
D	0016020	cellular_component	membrane
D	0020037	molecular_function	heme binding
D	1902600	biological_process	proton transmembrane transport
E	0004129	molecular_function	cytochrome-c oxidase activity
E	0005507	molecular_function	copper ion binding
E	0016020	cellular_component	membrane
E	0030313	cellular_component	cell envelope
E	1902600	biological_process	proton transmembrane transport

Functional Information from PROSITE/UniProt

site_id	PS00077
Number of Residues	57
Details	COX1_CUB Heme-copper oxidase catalytic subunit, copper B binding region signature. WFFGHPvVyfwllpayvalytilpkivsekgklysdpaarlafilflifslpvglHH

Chain	Residue	Details
A	TRP218-HIS274

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site_id	PS00078
Number of Residues	49
Details	COX2 CO II and nitrous oxide reductase dinuclear copper centers signature. VvHgvhihgtnynvmaipgtvgymrikfekpgvyhvv......ChefCgvgHhaM

Chain	Residue	Details
B	VAL94-MET142

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site_id	PS00430
Number of Residues	25
Details	TONB_DEPENDENT_REC_1 TonB-dependent receptor (TBDR) proteins signature 1. raektgltlalillltf..................................................................................................FSLIVYAA

Chain	Residue	Details
B	ARG3-ALA27

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