5CRH
Human skeletal calsequestrin, M53T mutant high-calcium complex
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005509 | molecular_function | calcium ion binding |
| A | 0005515 | molecular_function | protein binding |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0005759 | cellular_component | mitochondrial matrix |
| A | 0005783 | cellular_component | endoplasmic reticulum |
| A | 0005790 | cellular_component | smooth endoplasmic reticulum |
| A | 0007029 | biological_process | endoplasmic reticulum organization |
| A | 0007519 | biological_process | skeletal muscle tissue development |
| A | 0009408 | biological_process | response to heat |
| A | 0010880 | biological_process | regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum |
| A | 0014802 | cellular_component | terminal cisterna |
| A | 0014804 | cellular_component | terminal cisterna lumen |
| A | 0014809 | biological_process | regulation of skeletal muscle contraction by regulation of release of sequestered calcium ion |
| A | 0014870 | biological_process | response to muscle inactivity |
| A | 0014894 | biological_process | response to denervation involved in regulation of muscle adaptation |
| A | 0016020 | cellular_component | membrane |
| A | 0016529 | cellular_component | sarcoplasmic reticulum |
| A | 0030016 | cellular_component | myofibril |
| A | 0030018 | cellular_component | Z disc |
| A | 0030315 | cellular_component | T-tubule |
| A | 0031674 | cellular_component | I band |
| A | 0033017 | cellular_component | sarcoplasmic reticulum membrane |
| A | 0033018 | cellular_component | sarcoplasmic reticulum lumen |
| A | 0042383 | cellular_component | sarcolemma |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0045214 | biological_process | sarcomere organization |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0051258 | biological_process | protein polymerization |
| A | 0051281 | biological_process | positive regulation of release of sequestered calcium ion into cytosol |
| A | 0051282 | biological_process | regulation of sequestering of calcium ion |
| A | 1901341 | biological_process | positive regulation of store-operated calcium channel activity |
| A | 2001256 | biological_process | regulation of store-operated calcium entry |
| B | 0005509 | molecular_function | calcium ion binding |
| B | 0005515 | molecular_function | protein binding |
| B | 0005739 | cellular_component | mitochondrion |
| B | 0005759 | cellular_component | mitochondrial matrix |
| B | 0005783 | cellular_component | endoplasmic reticulum |
| B | 0005790 | cellular_component | smooth endoplasmic reticulum |
| B | 0007029 | biological_process | endoplasmic reticulum organization |
| B | 0007519 | biological_process | skeletal muscle tissue development |
| B | 0009408 | biological_process | response to heat |
| B | 0010880 | biological_process | regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum |
| B | 0014802 | cellular_component | terminal cisterna |
| B | 0014804 | cellular_component | terminal cisterna lumen |
| B | 0014809 | biological_process | regulation of skeletal muscle contraction by regulation of release of sequestered calcium ion |
| B | 0014870 | biological_process | response to muscle inactivity |
| B | 0014894 | biological_process | response to denervation involved in regulation of muscle adaptation |
| B | 0016020 | cellular_component | membrane |
| B | 0016529 | cellular_component | sarcoplasmic reticulum |
| B | 0030016 | cellular_component | myofibril |
| B | 0030018 | cellular_component | Z disc |
| B | 0030315 | cellular_component | T-tubule |
| B | 0031674 | cellular_component | I band |
| B | 0033017 | cellular_component | sarcoplasmic reticulum membrane |
| B | 0033018 | cellular_component | sarcoplasmic reticulum lumen |
| B | 0042383 | cellular_component | sarcolemma |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0045214 | biological_process | sarcomere organization |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0051258 | biological_process | protein polymerization |
| B | 0051281 | biological_process | positive regulation of release of sequestered calcium ion into cytosol |
| B | 0051282 | biological_process | regulation of sequestering of calcium ion |
| B | 1901341 | biological_process | positive regulation of store-operated calcium channel activity |
| B | 2001256 | biological_process | regulation of store-operated calcium entry |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | binding site for residue CA A 401 |
| Chain | Residue |
| A | ASP13 |
| A | VAL15 |
| A | GLU55 |
| A | GLU59 |
| A | HOH834 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue CA A 402 |
| Chain | Residue |
| A | HOH757 |
| A | HOH789 |
| A | GLU199 |
| A | THR229 |
| A | THR277 |
| A | HOH670 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue CA A 403 |
| Chain | Residue |
| A | ASP210 |
| A | PRO212 |
| A | GLU217 |
| A | HOH728 |
| A | HOH808 |
| A | HOH843 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | binding site for residue CA A 404 |
| Chain | Residue |
| A | THR189 |
| A | HOH636 |
| A | HOH655 |
| A | HOH660 |
| A | HOH762 |
| A | HOH841 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | binding site for residue CA A 405 |
| Chain | Residue |
| A | GLU91 |
| A | GLU105 |
| A | ASP107 |
| A | GLU240 |
| A | HOH601 |
| A | HOH676 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | binding site for residue CA A 406 |
| Chain | Residue |
| A | GLU91 |
| A | ASP107 |
| A | GLU243 |
| A | HOH613 |
| A | HOH772 |
| A | HOH827 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | binding site for residue CA A 407 |
| Chain | Residue |
| A | ASP113 |
| A | HOH740 |
| A | HOH821 |
| B | ASP113 |
| B | HOH558 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | binding site for residue CA A 408 |
| Chain | Residue |
| A | GLU117 |
| A | HOH637 |
| B | ASP290 |
| B | HOH716 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | binding site for residue CA A 409 |
| Chain | Residue |
| A | ASP121 |
| A | HOH544 |
| A | HOH753 |
| A | HOH773 |
| B | ASP290 |
| site_id | AD1 |
| Number of Residues | 6 |
| Details | binding site for residue CA A 410 |
| Chain | Residue |
| A | ASP165 |
| A | HOH656 |
| A | HOH675 |
| A | HOH693 |
| A | HOH783 |
| A | HOH936 |
| site_id | AD2 |
| Number of Residues | 6 |
| Details | binding site for residue CA A 411 |
| Chain | Residue |
| A | PRO172 |
| A | HOH519 |
| A | HOH532 |
| A | HOH606 |
| A | HOH859 |
| A | HOH896 |
| site_id | AD3 |
| Number of Residues | 6 |
| Details | binding site for residue CA A 412 |
| Chain | Residue |
| A | ASP259 |
| A | ASP261 |
| A | HOH547 |
| A | HOH638 |
| B | GLU128 |
| B | HOH694 |
| site_id | AD4 |
| Number of Residues | 6 |
| Details | binding site for residue CA A 413 |
| Chain | Residue |
| A | ASP261 |
| A | GLU331 |
| A | HOH534 |
| B | GLU135 |
| B | HOH542 |
| B | HOH611 |
| site_id | AD5 |
| Number of Residues | 6 |
| Details | binding site for residue CA A 414 |
| Chain | Residue |
| A | GLU264 |
| A | GLU331 |
| A | HOH529 |
| A | HOH567 |
| B | GLU135 |
| B | HOH628 |
| site_id | AD6 |
| Number of Residues | 6 |
| Details | binding site for residue CA A 415 |
| Chain | Residue |
| A | ASP290 |
| A | HOH525 |
| B | ASP121 |
| B | HOH548 |
| B | HOH625 |
| B | HOH644 |
| site_id | AD7 |
| Number of Residues | 5 |
| Details | binding site for residue CA A 416 |
| Chain | Residue |
| A | ASP290 |
| A | HOH743 |
| A | HOH811 |
| B | GLU117 |
| B | HOH709 |
| site_id | AD8 |
| Number of Residues | 5 |
| Details | binding site for residue CA A 417 |
| Chain | Residue |
| A | GLU128 |
| A | HOH518 |
| B | ASP259 |
| B | ASP261 |
| B | HOH680 |
| site_id | AD9 |
| Number of Residues | 6 |
| Details | binding site for residue CA A 418 |
| Chain | Residue |
| B | GLU331 |
| B | HOH522 |
| A | GLU135 |
| A | HOH604 |
| A | HOH726 |
| B | ASP261 |
| site_id | AE1 |
| Number of Residues | 7 |
| Details | binding site for residue CA A 419 |
| Chain | Residue |
| A | GLU135 |
| A | HOH580 |
| B | ASP261 |
| B | GLU264 |
| B | GLU331 |
| B | HOH523 |
| B | HOH723 |
| site_id | AE2 |
| Number of Residues | 6 |
| Details | binding site for residue CA B 401 |
| Chain | Residue |
| B | ASP13 |
| B | VAL15 |
| B | GLU55 |
| B | GLU59 |
| B | HOH683 |
| B | HOH703 |
| site_id | AE3 |
| Number of Residues | 5 |
| Details | binding site for residue CA B 402 |
| Chain | Residue |
| B | GLU199 |
| B | THR229 |
| B | THR277 |
| B | HOH584 |
| B | HOH710 |
| site_id | AE4 |
| Number of Residues | 4 |
| Details | binding site for residue CA B 403 |
| Chain | Residue |
| B | ASP210 |
| B | PRO212 |
| B | GLU217 |
| B | HOH658 |
| site_id | AE5 |
| Number of Residues | 5 |
| Details | binding site for residue CA B 404 |
| Chain | Residue |
| B | THR189 |
| B | HOH532 |
| B | HOH565 |
| B | HOH674 |
| B | HOH679 |
| site_id | AE6 |
| Number of Residues | 6 |
| Details | binding site for residue CA B 405 |
| Chain | Residue |
| B | GLU91 |
| B | GLU105 |
| B | ASP107 |
| B | GLU240 |
| B | HOH547 |
| B | HOH629 |
| site_id | AE7 |
| Number of Residues | 6 |
| Details | binding site for residue CA B 406 |
| Chain | Residue |
| B | GLU91 |
| B | ASP107 |
| B | GLU243 |
| B | HOH585 |
| B | HOH668 |
| B | HOH726 |
| site_id | AE8 |
| Number of Residues | 4 |
| Details | binding site for residue CA B 407 |
| Chain | Residue |
| B | PRO172 |
| B | HOH537 |
| B | HOH715 |
| B | HOH732 |
| site_id | AE9 |
| Number of Residues | 3 |
| Details | binding site for residue CA B 408 |
| Chain | Residue |
| B | ASP165 |
| B | HOH534 |
| B | HOH687 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P19633 |
| Chain | Residue | Details |
| A | TYR9 | |
| B | TYR9 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P19633 |
| Chain | Residue | Details |
| A | SER47 | |
| A | SER182 | |
| B | SER47 | |
| B | SER182 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P19633 |
| Chain | Residue | Details |
| A | THR90 | |
| B | THR90 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
| Chain | Residue | Details |
| A | ASN316 | |
| B | ASN316 |
