Structure of PDB 4ycm Chain A

Receptor sequence
>4ycmA (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
PDB4ycm Biselyngbyasides, cytotoxic marine macrolides, are novel and potent inhibitors of the Ca(2+) pumps with a unique mode of binding
ChainA
Resolution3.2 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 7BS A Q56 D59 N101 G105 K246 Q250 L253 I307 P308 L311 P312 I315 Q56 D59 N101 G105 K246 Q250 L253 I307 P308 L311 P312 I315 PDBbind-CN: -logKd/Ki=7.72,Ki=19nM
BindingDB: Ki=19nM
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:4ycm, PDBe:4ycm, PDBj:4ycm
PDBsum4ycm
PubMed25957767
UniProtP04191|AT2A1_RABIT Sarcoplasmic/endoplasmic reticulum calcium ATPase 1 (Gene Name=ATP2A1)

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