Structure of PDB 3n23 Chain A

Receptor sequence
>3n23A (length=992) Species: 9823 (Sus scrofa) [Search protein sequence]
MDELKKEVSMDDHKLSLDELHRKYGTDLSRGLTPARAAEILARDGPNALT
PPPTTPEWVKFCRQLFGGFSMLLWIGAILCFLAYGIQAATEEEPQNDNLY
LGVVLSAVVIITGCFSYYQEAKSSKIMESFKNMVPQQALVIRNGEKMSIN
AEEVVVGDLVEVKGGDRIPADLRIISANGCKVDNSSLTGESEPQTRSPDF
TNENPLETRNIAFFSTNCVEGTARGIVVYTGDRTVMGRIATLASGLEGGQ
TPIAAEIEHFIHIITGVAVFLGVSFFILSLILEYTWLEAVIFLIGIIVAN
VPEGLLATVTVCLTLTAKRMARKNCLVKNLEAVETLGSTSTICSDKTGTL
TQNRMTVAHMWSDNQIHEADTTENQSGVSFDKTSATWLALSRIAGLCNRA
VFQANQENLPILKRAVAGDASESALLKCIELCCGSVKEMRERYTKIVEIP
FNSTNKYQLSIHKNPNTAEPRHLLVMKGAPERILDRCSSILIHGKEQPLD
EELKDAFQNAYLELGGLGERVLGFCHLFLPDEQFPEGFQFDTDDVNFPLD
NLCFVGLISMIDPPRAAVPDAVGKCRSAGIKVIMVTGDHPITAKAIAKGV
GIISEGNETVEDIAARLNIPVSQVNPRDAKACVVHGSDLKDMTSEQLDDI
LKYHTEIVFARTSPQQKLIIVEGCQRQGAIVAVTGDGVNDSPASKKADIG
VAMGIAGSDVSKQAADMILLDDNFASIVTGVEEGRLIFDNLKKSIAYTLT
SNIPEITPFLIFIIANIPLPLGTVTILCIDLGTDMVPAISLAYEQAESDI
MKRQPRNPKTDKLVNEQLISMAYGQIGMIQALGGFFTYFVILAENGFLPI
HLLGLRVNWDDRWINDVEDSYGQQWTYEQRKIVEFTCHTPFFVTIVVVQW
ADLVICKTRRNSVFQQGMKNKILIFGLFEETALAAFLSYCPGMGVALRMY
PLKPTWWFCAFPYSLLIFVYDEVRKLIIRRRPGGWVEKETYY
3D structure
PDB3n23 Structural insights into the high affinity binding of cardiotonic steroids to the Na+,K+-ATPase.
ChainA
Resolution4.6 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D369 D710 D714
Catalytic site (residue number reindexed from 1) D345 D686 D690
Enzyme Commision number 7.2.2.13: Na(+)/K(+)-exchanging 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 OBN A P118 D121 V322 A323 F783 T797 R880 P94 D97 V298 A299 F759 T773 R856 PDBbind-CN: -logKd/Ki=8.52,Kd=3nM
BS02 MG A X369 T371 D710 G711 X345 T347 D686 G687
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0005215 transporter activity
GO:0005391 P-type sodium:potassium-exchanging transporter activity
GO:0005515 protein binding
GO:0005524 ATP binding
GO:0008556 P-type potassium transmembrane transporter activity
GO:0016887 ATP hydrolysis activity
GO:0030955 potassium ion binding
GO:0031402 sodium ion binding
GO:0046872 metal ion binding
GO:0051117 ATPase binding
Biological Process
GO:0002028 regulation of sodium ion transport
GO:0006813 potassium ion transport
GO:0006814 sodium ion transport
GO:0006883 intracellular sodium ion homeostasis
GO:0010248 establishment or maintenance of transmembrane electrochemical gradient
GO:0030007 intracellular potassium ion homeostasis
GO:0036376 sodium ion export across plasma membrane
GO:0055085 transmembrane transport
GO:0086009 membrane repolarization
GO:1902600 proton transmembrane transport
GO:1990573 potassium ion import across plasma membrane
Cellular Component
GO:0005886 plasma membrane
GO:0005890 sodium:potassium-exchanging ATPase complex
GO:0016020 membrane
GO:0016323 basolateral plasma membrane
GO:0030424 axon
GO:0042383 sarcolemma
GO:0042470 melanosome
GO:0042995 cell projection

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:3n23, PDBe:3n23, PDBj:3n23
PDBsum3n23
PubMed21182963
UniProtP05024|AT1A1_PIG Sodium/potassium-transporting ATPase subunit alpha-1 (Gene Name=ATP1A1)

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