Structure of PDB 5dn6 Chain A

Receptor sequence
>5dn6A (length=505) Species: 266 (Paracoccus denitrificans) [Search protein sequence]
GIQAAEISAILKDQIKNFGQDAEVAEVGQVLSVGDGIARVYGLDKVQAGE
MVEFPGGIRGMVLNLETDNVGVVIFGDDRDIKEGDTVKRTGAIVEVPAGK
ELLGRVVDALGNPIDGKGPLNASERRIADVKAPGIMPRKSVHEPMATGLK
SVDAMIPVGRGQRELIIGDRQTGKTAIALDTILNQANYNGMKTLHCIYVA
VGQKRSTVAQLVKKLEETGAMAYTTVVAATASDPAPMQYLAPYSATAMGE
YFRDNGMDALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRL
LERSAKLNEANGAGSLTALPIIETQAGDVSAYIPTNVISITDGQIFLETE
LFFQGIRPAVNTGLSVSRVGSAAQTKAMKSVAGPVKLELAQYREMAAFAQ
FGSDLDAATQKLLNRGARLTELMKQPQYSPLTNAEIVIVIYAGTKGYLDG
IPVRDVTKWEHGLLQYLRNQKADLLEDMTKNDRKVAGELEDAIKAALDGY
AKTYA
3D structure
PDB5dn6 Structure of ATP synthase from Paracoccus denitrificans determined by X-ray crystallography at 4.0 angstrom resolution.
ChainA
Resolution3.98 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 7.1.2.2: H(+)-transporting two-sector ATPase.
Interaction with ligand
Site
#
Ligand Ligand
chain
Binding residues on receptor
(original residue number in PDB)
Binding residues on receptor
(residue number reindexed from 1)
Binding affinity
BS01 ATP A R171 G174 K175 T176 A177 F358 Q433 R170 G173 K174 T175 A176 F352 Q427
Gene Ontology
Molecular Function
GO:0005524 ATP binding
GO:0032559 adenyl ribonucleotide binding
GO:0043531 ADP binding
GO:0046933 proton-transporting ATP synthase activity, rotational mechanism
GO:0046961 proton-transporting ATPase activity, rotational mechanism
Biological Process
GO:0006754 ATP biosynthetic process
GO:0015986 proton motive force-driven ATP synthesis
GO:0046034 ATP metabolic process
GO:1902600 proton transmembrane transport
Cellular Component
GO:0005886 plasma membrane
GO:0045259 proton-transporting ATP synthase complex
GO:0045261 proton-transporting ATP synthase complex, catalytic core F(1)

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:5dn6, PDBe:5dn6, PDBj:5dn6
PDBsum5dn6
PubMed26460036
UniProtA1B8N8|ATPA_PARDP ATP synthase subunit alpha (Gene Name=atpA)

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