Structure of PDB 6lle Chain A Binding Site BS01

Receptor Information
>6lle Chain A (length=1020) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MENAHTKTVEEVLGHFGVNESTGLSLEQVKKLKERWGSNELPAEEGKTLL
ELVIEQFEDLLVRILLLAACISFVLAWFEEGEETITAFVEPFVILLILVA
NAIVGVWQERNAENAIEALKEYEPEMGKVYRQDRKSVQRIKAKDIVPGDI
VEIAVGDKVPADIRLTSIKSTTLRVDQSILTGESVSVIKHTDPVPDPRAV
NQDKKNMLFSGTNIAAGKAMGVVVATGVNTEIGKIRDEMVATEQERTPLQ
QKLDEFGEQLSKVISLICIAVWIINIGHFNDPVHGGSWIRGAIYYFKIAV
ALAVAAIPEGLPAVITTCLALGTRRMAKKNAIVRSLPSVETLGCTSVICS
DKTGTLTTNQMSVCRMFILDRVEGDTCSLNEFTITGSTYAPIGEVHKDDK
PVNCHQYDGLVELATICALCNDSALDYNEAKGVYEKVGEATETALTCLVE
KMNVFDTELKGLSKIERANACNSVIKQLMKKEFTLEFSRDRKSMSVYCTP
NKPSSMSKMFVKGAPEGVIDRCTHIRVGSTKVPMTSGVKQKIMSVIREWG
SGSDTLRCLALATHDNPLRREEMHLEDSANFIKYETNLTFVGCVGMLDPP
RIEVASSVKLCRQAGIRVIMITGDNKGTAVAICRRIGIFGQDEDVTSKAF
TGREFDELNPSAQRDACLNARCFARVEPSHKSKIVEFLQSFDEITAMTGD
GVNDAPALKKAEIGIAMGSGTAVAKTASEMVLADDNFSTIVAAVEEGRAI
YNNMKQFIRYLISSNVGEVVCIFLTAALGFPEALIPVQLLWVNLVTDGLP
ATALGFNPPDLDIMNKPPRNPKEPLISGWLFFRYLAIGCYVGAATVGAAA
WWFIAADGGPRVSFYQLSHFLQCKEDNPDFEGVDCAIFESPYPMTMALSV
LVTIEMCNALNSLSENQSLLRMPPWENIWLVGSICLSMSLHFLILYVEPL
PLIFQITPLNVTQWLMVLKISLPVILMDETLKFVARNYLEGISWPFVLLI
MPLVIWVYSTDTNFSDMFWS
Ligand information
Ligand IDACP
InChIInChI=1S/C11H18N5O12P3/c12-9-6-10(14-2-13-9)16(3-15-6)11-8(18)7(17)5(27-11)1-26-31(24,25)28-30(22,23)4-29(19,20)21/h2-3,5,7-8,11,17-18H,1,4H2,(H,22,23)(H,24,25)(H2,12,13,14)(H2,19,20,21)/t5-,7-,8-,11-/m1/s1
InChIKeyUFZTZBNSLXELAL-IOSLPCCCSA-N
SMILES
SoftwareSMILES
CACTVS 3.341Nc1ncnc2n(cnc12)[CH]3O[CH](CO[P](O)(=O)O[P](O)(=O)C[P](O)(O)=O)[CH](O)[CH]3O
ACDLabs 10.04O=P(O)(O)CP(=O)(O)OP(=O)(O)OCC3OC(n2cnc1c(ncnc12)N)C(O)C3O
OpenEye OEToolkits 1.5.0c1nc(c2c(n1)n(cn2)C3C(C(C(O3)COP(=O)(O)OP(=O)(CP(=O)(O)O)O)O)O)N
OpenEye OEToolkits 1.5.0c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)CO[P@@](=O)(O)O[P@](=O)(CP(=O)(O)O)O)O)O)N
CACTVS 3.341Nc1ncnc2n(cnc12)[C@@H]3O[C@H](CO[P@](O)(=O)O[P@](O)(=O)C[P](O)(O)=O)[C@@H](O)[C@H]3O
FormulaC11 H18 N5 O12 P3
NamePHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER;
ADENOSINE-5'-[BETA, GAMMA-METHYLENE]TRIPHOSPHATE
ChEMBLCHEMBL133463
DrugBankDB03909
ZINCZINC000008295124
PDB chain6lle Chain A Residue 2001 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB6lle Cryo-EM structures of SERCA2b reveal the mechanism of regulation by the luminal extension tail.
Resolution2.9 Å
Binding residue
(original residue number in PDB)		D351 K352 T353 E439 E442 F487 R489 K514 G515 R559 T624 G625 D626 R677 K683 N705
Binding residue
(residue number reindexed from 1)		D351 K352 T353 E439 E442 F487 R489 K512 G513 R557 T622 G623 D624 R675 K681 N703
Annotation score3
Enzymatic activity
Enzyme Commision number 7.2.2.10: P-type Ca(2+) transporter.
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:0005515 protein binding
GO:0005524 ATP binding
GO:0016887 ATP hydrolysis activity
GO:0019899 enzyme binding
GO:0044325 transmembrane transporter binding
GO:0044548 S100 protein binding
GO:0046872 metal ion binding
GO:0086039 P-type calcium transporter activity involved in regulation of cardiac muscle cell membrane potential
GO:0106222 lncRNA binding
Biological Process
GO:0000045 autophagosome assembly
GO:0002026 regulation of the force of heart contraction
GO:0006816 calcium ion transport
GO:0006874 intracellular calcium ion homeostasis
GO:0006984 ER-nucleus signaling pathway
GO:0007155 cell adhesion
GO:0008544 epidermis development
GO:0010460 positive regulation of heart rate
GO:0010666 positive regulation of cardiac muscle cell apoptotic process
GO:0010882 regulation of cardiac muscle contraction by calcium ion signaling
GO:0014883 transition between fast and slow fiber
GO:0014898 cardiac muscle hypertrophy in response to stress
GO:0016240 autophagosome membrane docking
GO:0032469 endoplasmic reticulum calcium ion homeostasis
GO:0032470 positive regulation of endoplasmic reticulum calcium ion concentration
GO:0033292 T-tubule organization
GO:0034220 monoatomic ion transmembrane transport
GO:0034599 cellular response to oxidative stress
GO:0034976 response to endoplasmic reticulum stress
GO:0045822 negative regulation of heart contraction
GO:0070050 neuron cellular homeostasis
GO:0070296 sarcoplasmic reticulum calcium ion transport
GO:0070588 calcium ion transmembrane transport
GO:0086036 regulation of cardiac muscle cell membrane potential
GO:0098909 regulation of cardiac muscle cell action potential involved in regulation of contraction
GO:0140056 organelle localization by membrane tethering
GO:1900121 negative regulation of receptor binding
GO:1903233 regulation of calcium ion-dependent exocytosis of neurotransmitter
GO:1903515 calcium ion transport from cytosol to endoplasmic reticulum
GO:1903779 regulation of cardiac conduction
GO:1990036 calcium ion import into sarcoplasmic reticulum
GO:1990456 mitochondrion-endoplasmic reticulum membrane tethering
Cellular Component
GO:0005783 endoplasmic reticulum
GO:0005789 endoplasmic reticulum membrane
GO:0005886 plasma membrane
GO:0016020 membrane
GO:0016529 sarcoplasmic reticulum
GO:0031095 platelet dense tubular network membrane
GO:0033017 sarcoplasmic reticulum membrane
GO:0097470 ribbon synapse

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Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:6lle, PDBe:6lle, PDBj:6lle
PDBsum6lle
PubMed32851169
UniProtP16615|AT2A2_HUMAN Sarcoplasmic/endoplasmic reticulum calcium ATPase 2 (Gene Name=ATP2A2)

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