Structure of PDB 2xnd Chain C

Receptor sequence
>2xndC (length=492) Species: 9913 (Bos taurus) [Search protein sequence]
ADTSVDLEETGRVLSIGDGIARVHGLRNVQAEEMVEFSSGLKGMSLNLEP
DNVGVVVFGNDKLIKEGDIVKRTGAIVDVPVGEELLGRVVDALGNAIDGK
GPIGSKARRRVGLKAPGIIPRISVREPMQTGIKAVDSLVPIGRGQRELII
GDRQTGKTSIAIDTIINQKRFNDGTDEKKKLYCIYVAIGQKRSTVAQLVK
RLTDADAMKYTIVVSATASDAAPLQYLAPYSGCSMGEYFRDNGKHALIIY
DDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKMNDAFGG
GSLTALPVIETQAGDVSAYIPTNVISITDGQIFLETELFYKGIRPAINVG
LSVSRVGSAAQTRAMKQVAGTMKLELAQYREVAAFAQFGSDLDAATQQLL
SRGVRLTELLKQGQYSPMAIEEQVAVIYAGVRGYLDKLEPSKITKFENAF
LSHVISQHQALLGKIRTDGKISEESDAKLKEIVTNFLAGFEA
3D structure
PDB2xnd Bioenergetic Cost of Making an Adenosine Triphosphate Molecule in Animal Mitochondria.
ChainC
Resolution3.5 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) K175 Q208 K209 R373
Catalytic site (residue number reindexed from 1) K157 Q190 K191 R355
Enzyme Commision number 3.6.3.14: Transferred entry: 7.1.2.2.
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 ANP C R171 Q172 G174 K175 T176 S177 R362 Q432 R153 Q154 G156 K157 T158 S159 R344 Q414
BS02 ANP C S344 S372 R373 S326 S354 R355
Gene Ontology
Molecular Function
GO:0005524 ATP binding
GO:0032559 adenyl ribonucleotide binding
GO:0046933 proton-transporting ATP synthase activity, rotational mechanism
Biological Process
GO:0015986 proton motive force-driven ATP synthesis
GO:0046034 ATP metabolic process
GO:1902600 proton transmembrane transport
Cellular Component
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:2xnd, PDBe:2xnd, PDBj:2xnd
PDBsum2xnd
PubMed20847295
UniProtP19483|ATPA_BOVIN ATP synthase subunit alpha, mitochondrial (Gene Name=ATP5F1A)

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