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5GJV

Structure of the mammalian voltage-gated calcium channel Cav1.1 complex at near atomic resolution

Functional Information from GO Data
ChainGOidnamespacecontents
A0005216molecular_functionmonoatomic ion channel activity
A0005245molecular_functionvoltage-gated calcium channel activity
A0005262molecular_functioncalcium channel activity
A0005515molecular_functionprotein binding
A0005516molecular_functioncalmodulin binding
A0005886cellular_componentplasma membrane
A0005891cellular_componentvoltage-gated calcium channel complex
A0006811biological_processmonoatomic ion transport
A0006816biological_processcalcium ion transport
A0006936biological_processmuscle contraction
A0008331molecular_functionhigh voltage-gated calcium channel activity
A0016020cellular_componentmembrane
A0030315cellular_componentT-tubule
A0034220biological_processmonoatomic ion transmembrane transport
A0034702cellular_componentmonoatomic ion channel complex
A0044325molecular_functiontransmembrane transporter binding
A0045933biological_processpositive regulation of muscle contraction
A0046872molecular_functionmetal ion binding
A0051209biological_processrelease of sequestered calcium ion into cytosol
A0055085biological_processtransmembrane transport
A0060314biological_processregulation of ryanodine-sensitive calcium-release channel activity
A0070588biological_processcalcium ion transmembrane transport
A0071313biological_processcellular response to caffeine
A0098703biological_processcalcium ion import across plasma membrane
A1990454cellular_componentL-type voltage-gated calcium channel complex
B0005245molecular_functionvoltage-gated calcium channel activity
B0005891cellular_componentvoltage-gated calcium channel complex
B0070588biological_processcalcium ion transmembrane transport
C0005245molecular_functionvoltage-gated calcium channel activity
C0005891cellular_componentvoltage-gated calcium channel complex
C0070588biological_processcalcium ion transmembrane transport
E0005245molecular_functionvoltage-gated calcium channel activity
E0005246molecular_functioncalcium channel regulator activity
E0005262molecular_functioncalcium channel activity
E0005515molecular_functionprotein binding
E0005886cellular_componentplasma membrane
E0005891cellular_componentvoltage-gated calcium channel complex
E0006811biological_processmonoatomic ion transport
E0006816biological_processcalcium ion transport
E0016020cellular_componentmembrane
E0030315cellular_componentT-tubule
E0034220biological_processmonoatomic ion transmembrane transport
E0034702cellular_componentmonoatomic ion channel complex
E0042383cellular_componentsarcolemma
E0045933biological_processpositive regulation of muscle contraction
E0070588biological_processcalcium ion transmembrane transport
E1902514biological_processregulation of calcium ion transmembrane transport via high voltage-gated calcium channel
E1990454cellular_componentL-type voltage-gated calcium channel complex
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1049
DetailsTOPO_DOM: Extracellular => ECO:0000255
ChainResidueDetails
FGLU27-GLY1076
AVAL1061-SER1118
AALA1171-ASP1180
AGLU1251-PRO1268
AASP1382-PRO1873
EARG130-ASP134
EPRO205-HIS222
AGLY331-ARG432
ATYR484-SER494
ATHR543-SER561
AASN654-THR799
AMET851-ASN866
ALYS912-ASN930

site_idSWS_FT_FI2
Number of Residues20
DetailsTRANSMEM: Helical => ECO:0000255
ChainResidueDetails
FVAL1077-LEU1097
EALA109-PHE129
ETYR135-LEU155
ETRP180-LEU204

site_idSWS_FT_FI3
Number of Residues8
DetailsTOPO_DOM: Cytoplasmic => ECO:0000255
ChainResidueDetails
FVAL1098-LEU1106
AGLU886-VAL892
ALYS951-VAL1000
AARG1022-ARG1038
AHIS1141-HIS1148
AGLU1201-SER1231
AGLY1290-GLN1311
AALA1331-PHE1356
EGLU156-SER179
ALYS219-GLY279
AASN302-TRP309
AGLU452-HIS462
AGLU515-GLY523
AGLY582-PRO601
AILE624-PRO633
AGLU819-GLN830

site_idSWS_FT_FI4
Number of Residues3
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
FASP261
FSER263
FSER265

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P54290
ChainResidueDetails
FSER121

site_idSWS_FT_FI6
Number of Residues8
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
FASN94
FASN133
FASN186
FASN326
FASN350
FASN615
FASN784
FASN891

site_idSWS_FT_FI7
Number of Residues21
DetailsTRANSMEM: Helical; Name=S5 of repeat I => ECO:0000269|PubMed:27580036
ChainResidueDetails
APHE197-PHE218

site_idSWS_FT_FI8
Number of Residues80
DetailsINTRAMEM: Pore-forming => ECO:0000269|PubMed:26680202, ECO:0000269|PubMed:27580036
ChainResidueDetails
APHE280-VAL301
AGLN602-GLY623
ALEU1001-TYR1021
AALA1312-LEU1330

site_idSWS_FT_FI9
Number of Residues20
DetailsTRANSMEM: Helical; Name=S6 of repeat I => ECO:0000269|PubMed:27580036
ChainResidueDetails
APRO310-LEU330

site_idSWS_FT_FI10
Number of Residues18
DetailsTRANSMEM: Helical; Name=S1 of repeat II => ECO:0000269|PubMed:27580036
ChainResidueDetails
AVAL433-SER451

site_idSWS_FT_FI11
Number of Residues20
DetailsTRANSMEM: Helical; Name=S2 of repeat II => ECO:0000269|PubMed:27580036
ChainResidueDetails
ALEU463-MET483

site_idSWS_FT_FI12
Number of Residues19
DetailsTRANSMEM: Helical; Name=S3 of repeat II => ECO:0000269|PubMed:27580036
ChainResidueDetails
AILE495-VAL514

site_idSWS_FT_FI13
Number of Residues18
DetailsTRANSMEM: Helical; Name=S4 of repeat II => ECO:0000269|PubMed:27580036
ChainResidueDetails
AILE524-TRP542

site_idSWS_FT_FI14
Number of Residues19
DetailsTRANSMEM: Helical; Name=S5 of repeat II => ECO:0000269|PubMed:27580036
ChainResidueDetails
ALEU562-PHE581

site_idSWS_FT_FI15
Number of Residues19
DetailsTRANSMEM: Helical; Name=S6 of repeat II => ECO:0000269|PubMed:27580036
ChainResidueDetails
AGLY634-LEU653

site_idSWS_FT_FI16
Number of Residues18
DetailsTRANSMEM: Helical; Name=S1 of repeat III => ECO:0000269|PubMed:27580036
ChainResidueDetails
ATRP800-ALA818

site_idSWS_FT_FI17
Number of Residues19
DetailsTRANSMEM: Helical; Name=S2 of repeat III => ECO:0000269|PubMed:27580036
ChainResidueDetails
AILE831-LYS850

site_idSWS_FT_FI18
Number of Residues18
DetailsTRANSMEM: Helical; Name=S3 of repeat III => ECO:0000269|PubMed:27580036
ChainResidueDetails
ATYR867-LEU885

site_idSWS_FT_FI19
Number of Residues18
DetailsTRANSMEM: Helical; Name=S4 of repeat III => ECO:0000269|PubMed:27580036
ChainResidueDetails
AVAL893-ALA911

site_idSWS_FT_FI20
Number of Residues19
DetailsTRANSMEM: Helical; Name=S5 of repeat III => ECO:0000269|PubMed:27580036
ChainResidueDetails
AILE931-PHE950

site_idSWS_FT_FI21
Number of Residues21
DetailsTRANSMEM: Helical; Name=S6 of repeat III => ECO:0000269|PubMed:27580036
ChainResidueDetails
AVAL1039-PHE1060

site_idSWS_FT_FI22
Number of Residues21
DetailsTRANSMEM: Helical; Name=S1 of repeat IV => ECO:0000269|PubMed:27580036
ChainResidueDetails
ATYR1119-TYR1140

site_idSWS_FT_FI23
Number of Residues21
DetailsTRANSMEM: Helical; Name=S2 of repeat IV => ECO:0000269|PubMed:27580036
ChainResidueDetails
AILE1149-LEU1170

site_idSWS_FT_FI24
Number of Residues19
DetailsTRANSMEM: Helical; Name=S3 of repeat IV => ECO:0000269|PubMed:27580036
ChainResidueDetails
APRO1181-SER1200

site_idSWS_FT_FI25
Number of Residues18
DetailsTRANSMEM: Helical; Name=S4 of repeat IV => ECO:0000269|PubMed:27580036
ChainResidueDetails
ASER1232-ALA1250

site_idSWS_FT_FI26
Number of Residues20
DetailsTRANSMEM: Helical; Name=S5 of repeat IV => ECO:0000269|PubMed:27580036
ChainResidueDetails
ATYR1269-PHE1289

site_idSWS_FT_FI27
Number of Residues24
DetailsTRANSMEM: Helical; Name=S6 of repeat IV => ECO:0000269|PubMed:27580036
ChainResidueDetails
AALA1357-MET1381

site_idSWS_FT_FI28
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:27580036, ECO:0007744|PDB:5GJV
ChainResidueDetails
AGLU292
AGLU614
AGLU1014

site_idSWS_FT_FI29
Number of Residues1
DetailsSITE: Cleavage => ECO:0000305
ChainResidueDetails
APHE1690

site_idSWS_FT_FI30
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q02789
ChainResidueDetails
ASER393
ASER397

site_idSWS_FT_FI31
Number of Residues2
DetailsMOD_RES: Phosphoserine; by PKA => ECO:0000305|PubMed:2844809
ChainResidueDetails
ASER687
ASER1617

site_idSWS_FT_FI32
Number of Residues1
DetailsMOD_RES: Phosphoserine; by PKA and CAMK2 => ECO:0000305|PubMed:20937870
ChainResidueDetails
ASER1575

site_idSWS_FT_FI33
Number of Residues1
DetailsMOD_RES: Phosphothreonine; by CK2 => ECO:0000305|PubMed:20937870
ChainResidueDetails
ATHR1579

site_idSWS_FT_FI34
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN79

site_idSWS_FT_FI35
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0007744|PDB:5GJV
ChainResidueDetails
AASN257

218853

PDB entries from 2024-04-24

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