3TLM
Crystal Structure of Endoplasmic Reticulum Ca2+-ATPase (SERCA) From Bovine Muscle
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0005215 | molecular_function | transporter activity |
| A | 0005388 | molecular_function | P-type calcium transporter activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0006816 | biological_process | calcium ion transport |
| A | 0006874 | biological_process | intracellular calcium ion homeostasis |
| A | 0016020 | cellular_component | membrane |
| 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 | 0106134 | biological_process | positive regulation of cardiac muscle cell contraction |
| A | 1901896 | biological_process | positive regulation of ATPase-coupled calcium transmembrane transporter activity |
| A | 1902082 | biological_process | positive regulation of calcium ion import into sarcoplasmic reticulum |
| A | 1990036 | biological_process | calcium ion import into sarcoplasmic reticulum |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA A 1003 |
| Chain | Residue |
| A | VAL304 |
| A | ALA305 |
| A | ILE307 |
| A | GLU309 |
| A | ASN795 |
| A | ASP799 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA A 1004 |
| Chain | Residue |
| A | ASP799 |
| A | GLU907 |
| A | HOH1028 |
| A | ASN767 |
| A | GLU770 |
| A | THR798 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG A 1005 |
| Chain | Residue |
| A | ASP351 |
| A | THR353 |
| A | ASP702 |
| A | ACP1001 |
| A | HOH1011 |
| A | HOH1012 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE K A 1006 |
| Chain | Residue |
| A | LEU710 |
| A | LYS711 |
| A | ALA713 |
| A | GLU731 |
| site_id | AC5 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE ACP A 1001 |
| Chain | Residue |
| A | ASP351 |
| A | THR353 |
| A | GLU442 |
| A | PHE487 |
| A | ARG489 |
| A | LYS514 |
| A | GLY515 |
| A | ALA516 |
| A | ARG559 |
| A | LEU561 |
| A | THR624 |
| A | GLY625 |
| A | ASP626 |
| A | ARG677 |
| A | LYS683 |
| A | MG1005 |
| A | HOH1014 |
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:0000269|PubMed:22387132 |
| Chain | Residue | Details |
| A | MET1-SER48 | |
| 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:0000269|PubMed:22387132 |
| Chain | Residue | Details |
| A | LEU49-ALA69 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 108 |
| Details | TOPO_DOM: Lumenal => ECO:0000269|PubMed:22387132 |
| 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:0000269|PubMed:22387132 |
| Chain | Residue | Details |
| A | GLU90-ARG110 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 19 |
| Details | TRANSMEM: Helical; Name=3 => ECO:0000269|PubMed:22387132 |
| Chain | Residue | Details |
| A | ASP254-LEU273 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 17 |
| Details | TRANSMEM: Helical; Name=4 => ECO:0000269|PubMed:22387132 |
| Chain | Residue | Details |
| A | PHE296-ALA313 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 19 |
| Details | TRANSMEM: Helical; Name=5 => ECO:0000269|PubMed:22387132 |
| Chain | Residue | Details |
| A | LYS757-LEU776 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 20 |
| Details | TRANSMEM: Helical; Name=6 => ECO:0000269|PubMed:22387132 |
| Chain | Residue | Details |
| A | ILE787-GLY807 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 22 |
| Details | TRANSMEM: Helical; Name=7 => ECO:0000269|PubMed:22387132 |
| Chain | Residue | Details |
| A | ILE828-ALA850 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 19 |
| Details | TRANSMEM: Helical; Name=8 => ECO:0000269|PubMed:22387132 |
| Chain | Residue | Details |
| A | THR897-SER916 |
| site_id | SWS_FT_FI11 |
| Number of Residues | 18 |
| Details | TRANSMEM: Helical; Name=9 => ECO:0000269|PubMed:22387132 |
| Chain | Residue | Details |
| A | ILE930-TYR948 |
| site_id | SWS_FT_FI12 |
| Number of Residues | 20 |
| Details | TRANSMEM: Helical; Name=10 => ECO:0000269|PubMed:22387132 |
| Chain | Residue | Details |
| A | TYR964-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 | 19 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:22387132, ECO:0007744|PDB:3TLM |
| Chain | Residue | Details |
| A | VAL304 | |
| A | ARG559 | |
| A | THR624 | |
| A | GLY625 | |
| A | ARG677 | |
| A | ASP702 | |
| A | ASN767 | |
| A | GLU770 | |
| A | THR798 | |
| A | ASP799 | |
| A | GLU907 | |
| A | ALA305 | |
| A | ILE307 | |
| A | GLU309 | |
| A | ASP351 | |
| A | THR353 | |
| A | GLU442 | |
| A | ARG489 | |
| A | LYS514 |
| site_id | SWS_FT_FI15 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:P04191 |
| Chain | Residue | Details |
| A | ASP626 | |
| A | LYS683 | |
| A | ASN705 | |
| A | ASN795 |
| site_id | SWS_FT_FI16 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q64578 |
| Chain | Residue | Details |
| A | THR441 | |
| A | THR568 |
| site_id | SWS_FT_FI17 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q64578 |
| Chain | Residue | Details |
| A | SER580 |
