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7QBA

CryoEM structure of the ABC transporter NosDFY complexed with nitrous oxide reductase NosZ

Functional Information from GO Data
ChainGOidnamespacecontents
B0000166molecular_functionnucleotide binding
B0005524molecular_functionATP binding
B0005886cellular_componentplasma membrane
B0016787molecular_functionhydrolase activity
B0016887molecular_functionATP hydrolysis activity
C0000166molecular_functionnucleotide binding
C0005524molecular_functionATP binding
C0005886cellular_componentplasma membrane
C0016787molecular_functionhydrolase activity
C0016887molecular_functionATP hydrolysis activity
D0005886cellular_componentplasma membrane
E0005886cellular_componentplasma membrane
H0004129molecular_functioncytochrome-c oxidase activity
H0005507molecular_functioncopper ion binding
H0005509molecular_functioncalcium ion binding
H0016020cellular_componentmembrane
H0050304molecular_functionnitrous-oxide reductase activity
I0004129molecular_functioncytochrome-c oxidase activity
I0005507molecular_functioncopper ion binding
I0005509molecular_functioncalcium ion binding
I0016020cellular_componentmembrane
I0050304molecular_functionnitrous-oxide reductase activity
Functional Information from PROSITE/UniProt
site_idPS00078
Number of Residues49
DetailsCOX2 CO II and nitrous oxide reductase dinuclear copper centers signature. VsHgfvvvnhgvsmeispqqtssitfvadkpglhwyy......CswfChalHmeM
ChainResidueDetails
HVAL581-MET629

site_idPS00211
Number of Residues15
DetailsABC_TRANSPORTER_1 ABC transporters family signature. YSKGMRQRLGLAQAL
ChainResidueDetails
BTYR129-LEU143

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues28
DetailsRepeat: {"description":"PbH1 1","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues21
DetailsRepeat: {"description":"PbH1 2","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues29
DetailsRepeat: {"description":"PbH1 3","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues21
DetailsRepeat: {"description":"PbH1 4","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues21
DetailsRepeat: {"description":"PbH1 5","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues22
DetailsRepeat: {"description":"PbH1 6","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues21
DetailsRepeat: {"description":"PbH1 7","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues38
DetailsRepeat: {"description":"PbH1 8","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues448
DetailsDomain: {"description":"ABC transporter","evidences":[{"source":"PROSITE-ProRule","id":"PRU00434","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues14
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00434","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues240
DetailsTransmembrane: {"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues192
DetailsRegion: {"description":"COX2-like"}
ChainResidueDetails

site_idSWS_FT_FI13
Number of Residues40
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

246905

PDB entries from 2025-12-31

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