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5Z10

Structure of the mechanosensitive Piezo1 channel

Functional Information from GO Data
ChainGOidnamespacecontents
A0005261molecular_functionmonoatomic cation channel activity
A0005515molecular_functionprotein binding
A0005783cellular_componentendoplasmic reticulum
A0005789cellular_componentendoplasmic reticulum membrane
A0005886cellular_componentplasma membrane
A0006812biological_processmonoatomic cation transport
A0008381molecular_functionmechanosensitive monoatomic ion channel activity
A0010831biological_processpositive regulation of myotube differentiation
A0016020cellular_componentmembrane
A0031258cellular_componentlamellipodium membrane
A0033116cellular_componentendoplasmic reticulum-Golgi intermediate compartment membrane
A0033625biological_processpositive regulation of integrin activation
A0033634biological_processpositive regulation of cell-cell adhesion mediated by integrin
A0034220biological_processmonoatomic ion transmembrane transport
A0042391biological_processregulation of membrane potential
A0042802molecular_functionidentical protein binding
A0042995cellular_componentcell projection
A0050982biological_processdetection of mechanical stimulus
A0071260biological_processcellular response to mechanical stimulus
A0098655biological_processmonoatomic cation transmembrane transport
A0140135molecular_functionmechanosensitive monoatomic cation channel activity
B0005261molecular_functionmonoatomic cation channel activity
B0005515molecular_functionprotein binding
B0005783cellular_componentendoplasmic reticulum
B0005789cellular_componentendoplasmic reticulum membrane
B0005886cellular_componentplasma membrane
B0006812biological_processmonoatomic cation transport
B0008381molecular_functionmechanosensitive monoatomic ion channel activity
B0010831biological_processpositive regulation of myotube differentiation
B0016020cellular_componentmembrane
B0031258cellular_componentlamellipodium membrane
B0033116cellular_componentendoplasmic reticulum-Golgi intermediate compartment membrane
B0033625biological_processpositive regulation of integrin activation
B0033634biological_processpositive regulation of cell-cell adhesion mediated by integrin
B0034220biological_processmonoatomic ion transmembrane transport
B0042391biological_processregulation of membrane potential
B0042802molecular_functionidentical protein binding
B0042995cellular_componentcell projection
B0050982biological_processdetection of mechanical stimulus
B0071260biological_processcellular response to mechanical stimulus
B0098655biological_processmonoatomic cation transmembrane transport
B0140135molecular_functionmechanosensitive monoatomic cation channel activity
C0005261molecular_functionmonoatomic cation channel activity
C0005515molecular_functionprotein binding
C0005783cellular_componentendoplasmic reticulum
C0005789cellular_componentendoplasmic reticulum membrane
C0005886cellular_componentplasma membrane
C0006812biological_processmonoatomic cation transport
C0008381molecular_functionmechanosensitive monoatomic ion channel activity
C0010831biological_processpositive regulation of myotube differentiation
C0016020cellular_componentmembrane
C0031258cellular_componentlamellipodium membrane
C0033116cellular_componentendoplasmic reticulum-Golgi intermediate compartment membrane
C0033625biological_processpositive regulation of integrin activation
C0033634biological_processpositive regulation of cell-cell adhesion mediated by integrin
C0034220biological_processmonoatomic ion transmembrane transport
C0042391biological_processregulation of membrane potential
C0042802molecular_functionidentical protein binding
C0042995cellular_componentcell projection
C0050982biological_processdetection of mechanical stimulus
C0071260biological_processcellular response to mechanical stimulus
C0098655biological_processmonoatomic cation transmembrane transport
C0140135molecular_functionmechanosensitive monoatomic cation channel activity
Functional Information from PROSITE/UniProt
site_idPS00290
Number of Residues7
DetailsIG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YQCVAAH
ChainResidueDetails
ATYR1680-HIS1686

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2091
DetailsTRANSMEM: Helical => ECO:0000255
ChainResidueDetails
AVAL5-LEU25
ALEU520-VAL540
CALA2019-LEU2039
CALA2048-VAL2068
CALA2077-ILE2097
CTHR2145-ILE2165
CGLY2193-ILE2213
CLEU2458-GLY2478
ALEU577-VAL597
AILE608-TRP628
APHE635-PHE655
APHE687-PHE707
AVAL818-PHE838
APRO847-TYR867
ALEU921-TYR941
AILE982-ILE1002
AMET1006-ARG1023
APHE27-PRO47
ALEU1038-LEU1058
AVAL1155-THR1175
AILE1179-LEU1199
ALEU1207-LEU1227
ACYS1232-VAL1252
ALEU1272-LEU1292
AALA1678-ASN1698
AMET1700-LEU1720
AILE1734-TRP1754
AALA1978-PHE1998
AALA62-HIS82
AALA2019-LEU2039
AALA2048-VAL2068
AALA2077-ILE2097
ATHR2145-ILE2165
AGLY2193-ILE2213
ALEU2458-GLY2478
BVAL5-LEU25
BPHE27-PRO47
BALA62-HIS82
BARG120-GLY140
AARG120-GLY140
BLEU217-ILE237
BLEU250-LEU270
BTRP317-LEU337
BLEU435-LEU455
BHIS467-LEU487
BLEU520-VAL540
BLEU577-VAL597
BILE608-TRP628
BPHE635-PHE655
BPHE687-PHE707
ALEU217-ILE237
BVAL818-PHE838
BPRO847-TYR867
BLEU921-TYR941
BILE982-ILE1002
BMET1006-ARG1023
BLEU1038-LEU1058
BVAL1155-THR1175
BILE1179-LEU1199
BLEU1207-LEU1227
BCYS1232-VAL1252
ALEU250-LEU270
BLEU1272-LEU1292
BALA1678-ASN1698
BMET1700-LEU1720
BILE1734-TRP1754
BALA1978-PHE1998
BALA2019-LEU2039
BALA2048-VAL2068
BALA2077-ILE2097
BTHR2145-ILE2165
BGLY2193-ILE2213
ATRP317-LEU337
BLEU2458-GLY2478
CVAL5-LEU25
CPHE27-PRO47
CALA62-HIS82
CARG120-GLY140
CLEU217-ILE237
CLEU250-LEU270
CTRP317-LEU337
CLEU435-LEU455
CHIS467-LEU487
ALEU435-LEU455
CLEU520-VAL540
CLEU577-VAL597
CILE608-TRP628
CPHE635-PHE655
CPHE687-PHE707
CVAL818-PHE838
CPRO847-TYR867
CLEU921-TYR941
CILE982-ILE1002
CMET1006-ARG1023
AHIS467-LEU487
CLEU1038-LEU1058
CVAL1155-THR1175
CILE1179-LEU1199
CLEU1207-LEU1227
CCYS1232-VAL1252
CLEU1272-LEU1292
CALA1678-ASN1698
CMET1700-LEU1720
CILE1734-TRP1754
CALA1978-PHE1998

site_idSWS_FT_FI2
Number of Residues729
DetailsTOPO_DOM: Extracellular => ECO:0000269|PubMed:26390154
ChainResidueDetails
AARG2214-SER2457
BARG2214-SER2457
CARG2214-SER2457

site_idSWS_FT_FI3
Number of Residues3
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q0KL00
ChainResidueDetails
ASER758
BSER758
CSER758

site_idSWS_FT_FI4
Number of Residues3
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:19144319
ChainResidueDetails
ASER1385
BSER1385
CSER1385

site_idSWS_FT_FI5
Number of Residues3
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q92508
ChainResidueDetails
ASER1390
BSER1390
CSER1390

site_idSWS_FT_FI6
Number of Residues6
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:21183079
ChainResidueDetails
ASER1627
ASER1631
BSER1627
BSER1631
CSER1627
CSER1631

site_idSWS_FT_FI7
Number of Residues3
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079
ChainResidueDetails
ASER1646
BSER1646
CSER1646

site_idSWS_FT_FI8
Number of Residues6
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN94
AASN389
BASN94
BASN389
CASN94
CASN389

221716

PDB entries from 2024-06-26

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