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 | 0005783 | cellular_component | endoplasmic reticulum |
A | 0005789 | cellular_component | endoplasmic reticulum membrane |
A | 0006811 | biological_process | monoatomic ion transport |
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 | Topological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"22387132","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 20 |
Details | Transmembrane: {"description":"Helical; Name=1","evidences":[{"source":"PubMed","id":"22387132","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 63 |
Details | Topological domain: {"description":"Lumenal","evidences":[{"source":"PubMed","id":"22387132","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI4 |
Number of Residues | 20 |
Details | Transmembrane: {"description":"Helical; Name=2","evidences":[{"source":"PubMed","id":"22387132","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI5 |
Number of Residues | 19 |
Details | Transmembrane: {"description":"Helical; Name=3","evidences":[{"source":"PubMed","id":"22387132","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI6 |
Number of Residues | 17 |
Details | Transmembrane: {"description":"Helical; Name=4","evidences":[{"source":"PubMed","id":"22387132","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI7 |
Number of Residues | 19 |
Details | Transmembrane: {"description":"Helical; Name=5","evidences":[{"source":"PubMed","id":"22387132","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI8 |
Number of Residues | 20 |
Details | Transmembrane: {"description":"Helical; Name=6","evidences":[{"source":"PubMed","id":"22387132","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI9 |
Number of Residues | 22 |
Details | Transmembrane: {"description":"Helical; Name=7","evidences":[{"source":"PubMed","id":"22387132","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI10 |
Number of Residues | 19 |
Details | Transmembrane: {"description":"Helical; Name=8","evidences":[{"source":"PubMed","id":"22387132","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI11 |
Number of Residues | 18 |
Details | Transmembrane: {"description":"Helical; Name=9","evidences":[{"source":"PubMed","id":"22387132","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI12 |
Number of Residues | 20 |
Details | Transmembrane: {"description":"Helical; Name=10","evidences":[{"source":"PubMed","id":"22387132","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI13 |
Number of Residues | 31 |
Details | Region: {"description":"Interaction with PLN","evidences":[{"source":"UniProtKB","id":"P04191","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI14 |
Number of Residues | 1 |
Details | Active site: {"description":"4-aspartylphosphate intermediate","evidences":[{"source":"UniProtKB","id":"P04191","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI15 |
Number of Residues | 19 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"22387132","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3TLM","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI16 |
Number of Residues | 4 |
Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P04191","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI17 |
Number of Residues | 2 |
Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"Q64578","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI18 |
Number of Residues | 1 |
Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q64578","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |