6LN6
CryoEM structure of SERCA2b T1032stop in E1-2Ca2+-AMPPCP (class2)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000045 | biological_process | autophagosome assembly |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0002026 | biological_process | regulation of the force of heart contraction |
| A | 0005215 | molecular_function | transporter activity |
| A | 0005388 | molecular_function | P-type calcium transporter activity |
| A | 0005509 | molecular_function | calcium ion binding |
| A | 0005515 | molecular_function | protein binding |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005783 | cellular_component | endoplasmic reticulum |
| A | 0005789 | cellular_component | endoplasmic reticulum membrane |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0006816 | biological_process | calcium ion transport |
| A | 0006874 | biological_process | intracellular calcium ion homeostasis |
| A | 0006984 | biological_process | ER-nucleus signaling pathway |
| A | 0007155 | biological_process | cell adhesion |
| A | 0008544 | biological_process | epidermis development |
| A | 0010460 | biological_process | positive regulation of heart rate |
| A | 0010666 | biological_process | positive regulation of cardiac muscle cell apoptotic process |
| A | 0010882 | biological_process | regulation of cardiac muscle contraction by calcium ion signaling |
| A | 0014883 | biological_process | transition between fast and slow fiber |
| A | 0014898 | biological_process | cardiac muscle hypertrophy in response to stress |
| A | 0016020 | cellular_component | membrane |
| A | 0016240 | biological_process | autophagosome membrane docking |
| A | 0016529 | cellular_component | sarcoplasmic reticulum |
| A | 0016887 | molecular_function | ATP hydrolysis activity |
| A | 0019899 | molecular_function | enzyme binding |
| A | 0031095 | cellular_component | platelet dense tubular network membrane |
| A | 0032469 | biological_process | endoplasmic reticulum calcium ion homeostasis |
| A | 0032470 | biological_process | positive regulation of endoplasmic reticulum calcium ion concentration |
| A | 0033017 | cellular_component | sarcoplasmic reticulum membrane |
| A | 0033292 | biological_process | T-tubule organization |
| A | 0034220 | biological_process | monoatomic ion transmembrane transport |
| A | 0034599 | biological_process | cellular response to oxidative stress |
| A | 0034976 | biological_process | response to endoplasmic reticulum stress |
| A | 0044325 | molecular_function | transmembrane transporter binding |
| A | 0044548 | molecular_function | S100 protein binding |
| A | 0045822 | biological_process | negative regulation of heart contraction |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0070050 | biological_process | neuron cellular homeostasis |
| A | 0070296 | biological_process | sarcoplasmic reticulum calcium ion transport |
| A | 0070588 | biological_process | calcium ion transmembrane transport |
| A | 0086036 | biological_process | regulation of cardiac muscle cell membrane potential |
| A | 0086039 | molecular_function | P-type calcium transporter activity involved in regulation of cardiac muscle cell membrane potential |
| A | 0097470 | cellular_component | ribbon synapse |
| A | 0098909 | biological_process | regulation of cardiac muscle cell action potential involved in regulation of contraction |
| A | 0106222 | molecular_function | lncRNA binding |
| A | 0140056 | biological_process | organelle localization by membrane tethering |
| A | 1900121 | biological_process | negative regulation of receptor binding |
| A | 1903233 | biological_process | regulation of calcium ion-dependent exocytosis of neurotransmitter |
| A | 1903515 | biological_process | calcium ion transport from cytosol to endoplasmic reticulum |
| A | 1903779 | biological_process | regulation of cardiac conduction |
| A | 1990036 | biological_process | calcium ion import into sarcoplasmic reticulum |
| A | 1990456 | biological_process | mitochondrion-endoplasmic reticulum membrane tethering |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 17 |
| Details | binding site for residue ACP A 2001 |
| Chain | Residue |
| A | ASP351 |
| A | ARG559 |
| A | THR624 |
| A | GLY625 |
| A | ASP626 |
| A | ARG677 |
| A | LYS683 |
| A | ASN705 |
| A | MG2002 |
| A | LYS352 |
| A | THR353 |
| A | GLU442 |
| A | PHE487 |
| A | ARG489 |
| A | LYS492 |
| A | LYS514 |
| A | GLY515 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue MG A 2002 |
| Chain | Residue |
| A | ASP351 |
| A | THR353 |
| A | ASP702 |
| A | ASP706 |
| A | ACP2001 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue CA A 2003 |
| Chain | Residue |
| A | VAL304 |
| A | ALA305 |
| A | ILE307 |
| A | GLU309 |
| A | ASN795 |
| A | ASP799 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | binding site for residue CA A 2004 |
| Chain | Residue |
| A | ASN767 |
| A | GLU770 |
| A | THR798 |
| A | ASP799 |
| A | GLU907 |
Functional Information from PROSITE/UniProt
| site_id | PS00154 |
| Number of Residues | 7 |
| Details | ATPASE_E1_E2 E1-E2 ATPases phosphorylation site. DKTGTLT |
| Chain | Residue | Details |
| A | ASP351-THR357 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 662 |
| Details | TOPO_DOM: Cytoplasmic => ECO:0000305 |
| Chain | Residue | Details |
| A | MET1-THR48 | |
| A | ASN111-LEU253 | |
| A | VAL314-MET756 | |
| A | PHE808-LEU827 | |
| A | GLU917-ASN929 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 20 |
| Details | TRANSMEM: Helical; Name=1 => ECO:0000250|UniProtKB:P04191 |
| Chain | Residue | Details |
| A | LEU49-ALA69 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 108 |
| Details | TOPO_DOM: Lumenal => ECO:0000305 |
| Chain | Residue | Details |
| A | CYS70-VAL89 | |
| A | ILE274-TYR295 | |
| A | THR777-LEU786 | |
| A | ALA851-MET896 | |
| A | VAL949-VAL963 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 20 |
| Details | TRANSMEM: Helical; Name=2 => ECO:0000250|UniProtKB:P04191 |
| Chain | Residue | Details |
| A | GLU90-ARG110 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 19 |
| Details | TRANSMEM: Helical; Name=3 => ECO:0000250|UniProtKB:P04191 |
| Chain | Residue | Details |
| A | ASP254-ILE273 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 17 |
| Details | TRANSMEM: Helical; Name=4 => ECO:0000250|UniProtKB:P04191 |
| Chain | Residue | Details |
| A | PHE296-ALA313 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 19 |
| Details | TRANSMEM: Helical; Name=5 => ECO:0000250|UniProtKB:P04191 |
| Chain | Residue | Details |
| A | LYS757-LEU776 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 20 |
| Details | TRANSMEM: Helical; Name=6 => ECO:0000250|UniProtKB:P04191 |
| Chain | Residue | Details |
| A | ILE787-GLY807 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 22 |
| Details | TRANSMEM: Helical; Name=7 => ECO:0000250|UniProtKB:P04191 |
| Chain | Residue | Details |
| A | ILE828-ALA850 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 19 |
| Details | TRANSMEM: Helical; Name=8 => ECO:0000250|UniProtKB:P04191 |
| Chain | Residue | Details |
| A | THR897-SER916 |
| site_id | SWS_FT_FI11 |
| Number of Residues | 18 |
| Details | TRANSMEM: Helical; Name=9 => ECO:0000250|UniProtKB:P04191 |
| Chain | Residue | Details |
| A | ILE930-TYR948 |
| site_id | SWS_FT_FI12 |
| Number of Residues | 20 |
| Details | TRANSMEM: Helical; Name=10 => ECO:0000250|UniProtKB:P04191 |
| Chain | Residue | Details |
| A | THR964-LYS984 |
| site_id | SWS_FT_FI13 |
| Number of Residues | 1 |
| Details | ACT_SITE: 4-aspartylphosphate intermediate => ECO:0000250|UniProtKB:P04191 |
| Chain | Residue | Details |
| A | ASP351 |
| site_id | SWS_FT_FI14 |
| Number of Residues | 18 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:P11607 |
| Chain | Residue | Details |
| A | VAL304 | |
| A | ASP626 | |
| A | ARG677 | |
| A | ASP702 | |
| A | ASN705 | |
| A | ASN767 | |
| A | GLU770 | |
| A | ASN795 | |
| A | THR798 | |
| A | ASP799 | |
| A | ALA305 | |
| A | ILE307 | |
| A | GLU309 | |
| A | ASP351 | |
| A | THR353 | |
| A | GLU442 | |
| A | ARG489 | |
| A | LYS514 |
| site_id | SWS_FT_FI15 |
| Number of Residues | 5 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:P04191 |
| Chain | Residue | Details |
| A | ARG559 | |
| A | THR624 | |
| A | GLY625 | |
| A | LYS683 | |
| A | GLU907 |
| site_id | SWS_FT_FI16 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:O55143 |
| Chain | Residue | Details |
| A | SER38 | |
| A | SER531 |
| site_id | SWS_FT_FI17 |
| Number of Residues | 2 |
| Details | MOD_RES: 3'-nitrotyrosine => ECO:0000269|PubMed:16399855 |
| Chain | Residue | Details |
| A | TYR294 | |
| A | TYR295 |
| site_id | SWS_FT_FI18 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q64578 |
| Chain | Residue | Details |
| A | THR441 |
| site_id | SWS_FT_FI19 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569 |
| Chain | Residue | Details |
| A | SER580 |
| site_id | SWS_FT_FI20 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569 |
| Chain | Residue | Details |
| A | SER663 |
