6HXB
SERCA2a from pig heart
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000045 | biological_process | autophagosome assembly |
A | 0000166 | molecular_function | nucleotide binding |
A | 0005215 | molecular_function | transporter activity |
A | 0005388 | molecular_function | P-type calcium transporter activity |
A | 0005515 | molecular_function | protein binding |
A | 0005524 | molecular_function | ATP binding |
A | 0006816 | biological_process | calcium ion transport |
A | 0006874 | biological_process | intracellular calcium ion homeostasis |
A | 0010882 | biological_process | regulation of cardiac muscle contraction by calcium ion signaling |
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 | 0033017 | cellular_component | sarcoplasmic reticulum membrane |
A | 0046872 | molecular_function | metal ion binding |
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 | 0140056 | biological_process | organelle localization by membrane tethering |
A | 1990456 | biological_process | mitochondrion-endoplasmic reticulum membrane tethering |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | binding site for residue CA A 1001 |
Chain | Residue |
A | ASN767 |
A | GLU770 |
A | THR798 |
A | ASP799 |
site_id | AC2 |
Number of Residues | 6 |
Details | binding site for residue CA A 1002 |
Chain | Residue |
A | ASP799 |
A | VAL304 |
A | ALA305 |
A | ILE307 |
A | GLU309 |
A | ASN795 |
site_id | AC3 |
Number of Residues | 5 |
Details | binding site for residue CA A 1003 |
Chain | Residue |
A | ASP351 |
A | THR353 |
A | ASP702 |
A | ACP1004 |
A | HOH1101 |
site_id | AC4 |
Number of Residues | 17 |
Details | binding site for residue ACP A 1004 |
Chain | Residue |
A | ASP351 |
A | THR353 |
A | GLU442 |
A | PHE487 |
A | ARG489 |
A | LYS514 |
A | GLY515 |
A | ARG559 |
A | CYS560 |
A | LEU561 |
A | THR624 |
A | ASP626 |
A | ARG677 |
A | ASP702 |
A | ASN705 |
A | CA1003 |
A | HOH1101 |
site_id | AC5 |
Number of Residues | 4 |
Details | binding site for residue K A 1005 |
Chain | Residue |
A | LEU710 |
A | LYS711 |
A | SER713 |
A | GLU731 |
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-LEU963 |
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 | 15 |
Details | BINDING: BINDING => ECO:0000305|PubMed:30777856, ECO:0007744|PDB:6HXB |
Chain | Residue | Details |
A | VAL304 | |
A | ASN705 | |
A | ASN767 | |
A | GLU770 | |
A | ASN795 | |
A | THR798 | |
A | ASP799 | |
A | ALA305 | |
A | ILE307 | |
A | GLU309 | |
A | GLU442 | |
A | ARG489 | |
A | LYS514 | |
A | ASP626 | |
A | ARG677 |
site_id | SWS_FT_FI15 |
Number of Residues | 3 |
Details | BINDING: BINDING => ECO:0000269|PubMed:30777856, ECO:0007744|PDB:5MPM |
Chain | Residue | Details |
A | ASP351 | |
A | THR353 | |
A | ASP702 |
site_id | SWS_FT_FI16 |
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_FI17 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:O55143 |
Chain | Residue | Details |
A | SER38 | |
A | SER531 |
site_id | SWS_FT_FI18 |
Number of Residues | 2 |
Details | MOD_RES: 3'-nitrotyrosine => ECO:0000250|UniProtKB:P16615 |
Chain | Residue | Details |
A | TYR294 | |
A | TYR295 |
site_id | SWS_FT_FI19 |
Number of Residues | 1 |
Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q64578 |
Chain | Residue | Details |
A | THR441 |
site_id | SWS_FT_FI20 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P16615 |
Chain | Residue | Details |
A | SER580 | |
A | SER663 |