Structure of PDB 6hef Chain A

Receptor sequence
>6hefA (length=994) Species: 9986 (Oryctolagus cuniculus) [Search protein sequence]
MEAAHSKSTEECLAYFGVSETTGLTPDQVKRHLEKYGHNELPAEEGKSLW
ELVIEQFEDLLVRILLLAACISFVLAWFEEGEETITAFVEPFVILLILIA
NAIVGVWQERNAENAIEALKEYEPEMGKVYRADRKSVQRIKARDIVPGDI
VEVAVGDKVPADIRILSIKSTTLRVDQSILTGESVSVIKHTEPVPDPRAV
NQDKKNMLFSGTNIAAGKALGIVATTGVSTEIGKIRDQMAATEQDKTPLQ
QKLDEFGEQLSKVISLICVAVWLINIGHFNDPVHGGSWIRGAIYYFKIAV
ALAVAAIPEGLPAVITTCLALGTRRMAKKNAIVRSLPSVETLGCTSVICS
DKTGTLTTNQMSVCKMFIIDKVDGDFCSLNEFSITGSTYAPEGEVLKNDK
PIRSGQFDGLVELATICALCNDSSLDFNETKGVYEKVGEATETALTTLVE
KMNVFNTEVRNLSKVERANACNSVIRQLMKKEFTLEFSRDRKSMSVYCSP
AKSSRAAVGNKMFVKGAPEGVIDRCNYVRVGTTRVPMTGPVKEKILSVIK
EWGTGRDTLRCLALATRDTPPKREEMVLDDSSRFMEYETDLTFVGVVGML
DPPRKEVMGSIQLCRDAGIRVIMITGDNKGTAIAICRRIGIFGENEEVAD
RAYTGREFDDLPLAEQREACRRACCFARVEPSHKSKIVEYLQSYDEITAM
TGDGVNDAPALKKAEIGIAMGSGTAVAKTASEMVLADDNFSTIVAAVEEG
RAIYNNMKQFIRYLISSNVGEVVCIFLTAALGLPEALIPVQLLWVNLVTD
GLPATALGFNPPDLDIMDRPPRSPKEPLISGWLFFRYMAIGGYVGAATVG
AAAWWFMYAEDGPGVTYHQLTHFMQCTEDHPHFEGLDCEIFEAPEPMTMA
LSVLVTIEMCNALNSLSENQSLMRMPPWVNIWLLGSICLSMSLHFLILYV
DPLPMIFKLKALDLTQWLMVLKISLPVIGLDEILKFIARNYLEG
3D structure
PDB6hef Membrane-protein crystals for neutron diffraction.
ChainA
Resolution3.538 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D351 D703 D707
Catalytic site (residue number reindexed from 1) D351 D703 D707
Enzyme Commision number 7.2.2.10: P-type Ca(2+) transporter.
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 ACP A D351 T353 E442 F487 R489 K492 M494 K515 R560 G626 N706 D351 T353 E442 F487 R489 K492 M494 K515 R560 G626 N706
BS02 CA A D351 T353 D703 D351 T353 D703
BS03 CA A V304 A305 I307 E309 N796 D800 V304 A305 I307 E309 N796 D800
BS04 CA A N768 E771 T799 D800 E908 N768 E771 T799 D800 E908
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0005215 transporter activity
GO:0005388 P-type calcium transporter activity
GO:0005509 calcium ion binding
GO:0005524 ATP binding
GO:0016887 ATP hydrolysis activity
GO:0046872 metal ion binding
Biological Process
GO:0006816 calcium ion transport
GO:0006874 intracellular calcium ion homeostasis
GO:0031448 positive regulation of fast-twitch skeletal muscle fiber contraction
GO:0070588 calcium ion transmembrane transport
GO:0106134 positive regulation of cardiac muscle cell contraction
GO:1901896 positive regulation of ATPase-coupled calcium transmembrane transporter activity
GO:1902082 positive regulation of calcium ion import into sarcoplasmic reticulum
GO:1990036 calcium ion import into sarcoplasmic reticulum
Cellular Component
GO:0016020 membrane
GO:0016529 sarcoplasmic reticulum
GO:0033017 sarcoplasmic reticulum membrane

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:6hef, PDBe:6hef, PDBj:6hef
PDBsum6hef
PubMed30605135
UniProtP04191|AT2A1_RABIT Sarcoplasmic/endoplasmic reticulum calcium ATPase 1 (Gene Name=ATP2A1)

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