Structure of PDB 2agv Chain B

Receptor sequence
>2agvB (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
PDB2agv Inaugural Article: Structural role of countertransport revealed in Ca2+ pump crystal structure in the absence of Ca2+.
ChainB
Resolution2.4 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 TG1 B F256 Q259 L260 V263 I267 I765 V769 V772 F776 I829 F834 Y837 M838 F256 Q259 L260 V263 I267 I765 V769 V772 F776 I829 F834 Y837 M838 BindingDB: Kd=0.200000nM,IC50=0.2nM
BS02 BHQ B D59 L61 V62 L65 F256 P308 L311 P312 D59 L61 V62 L65 F256 P308 L311 P312 MOAD: Kd=20nM
BindingDB: IC50=2000nM
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:2agv, PDBe:2agv, PDBj:2agv
PDBsum2agv
PubMed16150713
UniProtP04191|AT2A1_RABIT Sarcoplasmic/endoplasmic reticulum calcium ATPase 1 (Gene Name=ATP2A1)

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