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8FD7

Structure of the human L-type voltage-gated calcium channel Cav1.2 complexed with gabapentin

Functional Information from GO Data
ChainGOidnamespacecontents
C0005245molecular_functionvoltage-gated calcium channel activity
C0005246molecular_functioncalcium channel regulator activity
C0005262molecular_functioncalcium channel activity
C0005737cellular_componentcytoplasm
C0005891cellular_componentvoltage-gated calcium channel complex
C0034702cellular_componentmonoatomic ion channel complex
C0061577biological_processcalcium ion transmembrane transport via high voltage-gated calcium channel
C0070588biological_processcalcium ion transmembrane transport
C1901843biological_processpositive regulation of high voltage-gated calcium channel activity
C1990454cellular_componentL-type voltage-gated calcium channel complex
K0005216molecular_functionmonoatomic ion channel activity
K0005245molecular_functionvoltage-gated calcium channel activity
K0005891cellular_componentvoltage-gated calcium channel complex
K0006811biological_processmonoatomic ion transport
K0016020cellular_componentmembrane
K0055085biological_processtransmembrane transport
K0070588biological_processcalcium ion transmembrane transport
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P54287
ChainResidueDetails
CSER152
KLEU1182-GLN1239
KVAL1292-THR1301
KGLU1392-LEU1409
CSER393
KPRO252-LEU268
KGLY402-ASN524
KTYR576-SER586
KASN635-SER653
KASN746-THR900
KTHR953-GLN987
KVAL1033-PHE1051

site_idSWS_FT_FI2
Number of Residues18
DetailsTRANSMEM: Helical; Name=S1 of repeat I => ECO:0000250|UniProtKB:P07293
ChainResidueDetails
KPRO125-ILE143

site_idSWS_FT_FI3
Number of Residues335
DetailsTOPO_DOM: Extracellular => ECO:0000305
ChainResidueDetails
KTYR144-ASN158
KARG1007-LYS1013
KASN1072-LEU1121
KSER1143-ASN1159
KPHE1262-LYS1269
KARG1322-PHE1372
KCYS1431-ALA1452
KVAL1472-ARG1499
KALA210-ASP232
KMET291-ALA350
KASN373-TRP380
KGLU544-GLU554
KGLU607-GLY615
KGLY674-PRO693
KILE716-PRO725
KGLU920-HIS931

site_idSWS_FT_FI4
Number of Residues20
DetailsTRANSMEM: Helical; Name=S2 of repeat I => ECO:0000250|UniProtKB:P07293
ChainResidueDetails
KLEU159-ILE179
DSER263
DSER265

site_idSWS_FT_FI5
Number of Residues20
DetailsTRANSMEM: Helical; Name=S3 of repeat I => ECO:0000250|UniProtKB:P07293
ChainResidueDetails
KALA189-SER209

site_idSWS_FT_FI6
Number of Residues18
DetailsTRANSMEM: Helical; Name=S4 of repeat I => ECO:0000250|UniProtKB:P07293
ChainResidueDetails
KVAL233-VAL251
DASN138
DASN186
DASN326
DASN350
DASN615
DLYS784
DILE891

site_idSWS_FT_FI7
Number of Residues21
DetailsTRANSMEM: Helical; Name=S5 of repeat I => ECO:0000250|UniProtKB:P07293
ChainResidueDetails
KLEU269-PHE290

site_idSWS_FT_FI8
Number of Residues80
DetailsINTRAMEM: Pore-forming => ECO:0000250|UniProtKB:P07293
ChainResidueDetails
KPHE351-VAL372
KGLN694-GLY715
KTYR1122-ILE1142
KVAL1453-PHE1471

site_idSWS_FT_FI9
Number of Residues20
DetailsTRANSMEM: Helical; Name=S6 of repeat I => ECO:0000250|UniProtKB:P07293
ChainResidueDetails
KPRO381-LEU401

site_idSWS_FT_FI10
Number of Residues18
DetailsTRANSMEM: Helical; Name=S1 of repeat II => ECO:0000250|UniProtKB:P07293
ChainResidueDetails
KVAL525-SER543

site_idSWS_FT_FI11
Number of Residues20
DetailsTRANSMEM: Helical; Name=S2 of repeat II => ECO:0000250|UniProtKB:P07293
ChainResidueDetails
KVAL555-MET575

site_idSWS_FT_FI12
Number of Residues19
DetailsTRANSMEM: Helical; Name=S3 of repeat II => ECO:0000250|UniProtKB:P07293
ChainResidueDetails
KLEU587-VAL606

site_idSWS_FT_FI13
Number of Residues18
DetailsTRANSMEM: Helical; Name=S4 of repeat II => ECO:0000250|UniProtKB:P07293
ChainResidueDetails
KILE616-TRP634

site_idSWS_FT_FI14
Number of Residues19
DetailsTRANSMEM: Helical; Name=S5 of repeat II => ECO:0000250|UniProtKB:P07293
ChainResidueDetails
KLEU654-PHE673

site_idSWS_FT_FI15
Number of Residues19
DetailsTRANSMEM: Helical; Name=S6 of repeat II => ECO:0000250|UniProtKB:P07293
ChainResidueDetails
KGLY726-LEU745

site_idSWS_FT_FI16
Number of Residues18
DetailsTRANSMEM: Helical; Name=S1 of repeat III => ECO:0000250|UniProtKB:P07293
ChainResidueDetails
KILE901-ALA919

site_idSWS_FT_FI17
Number of Residues20
DetailsTRANSMEM: Helical; Name=S2 of repeat III => ECO:0000255
ChainResidueDetails
KILE932-MET952

site_idSWS_FT_FI18
Number of Residues18
DetailsTRANSMEM: Helical; Name=S3 of repeat III => ECO:0000250|UniProtKB:P07293
ChainResidueDetails
KSER988-LEU1006

site_idSWS_FT_FI19
Number of Residues18
DetailsTRANSMEM: Helical; Name=S4 of repeat III => ECO:0000250|UniProtKB:P07293
ChainResidueDetails
KGLY1014-ILE1032

site_idSWS_FT_FI20
Number of Residues19
DetailsTRANSMEM: Helical; Name=S5 of repeat III => ECO:0000250|UniProtKB:P07293
ChainResidueDetails
KLYS1052-GLY1071

site_idSWS_FT_FI21
Number of Residues21
DetailsTRANSMEM: Helical; Name=S6 of repeat III => ECO:0000250|UniProtKB:P07293
ChainResidueDetails
KILE1160-GLU1181

site_idSWS_FT_FI22
Number of Residues21
DetailsTRANSMEM: Helical; Name=S1 of repeat IV => ECO:0000250|UniProtKB:P07293
ChainResidueDetails
KHIS1240-LEU1261

site_idSWS_FT_FI23
Number of Residues21
DetailsTRANSMEM: Helical; Name=S2 of repeat IV => ECO:0000250|UniProtKB:P07293
ChainResidueDetails
KLEU1270-VAL1291

site_idSWS_FT_FI24
Number of Residues19
DetailsTRANSMEM: Helical; Name=S3 of repeat IV => ECO:0000250|UniProtKB:P07293
ChainResidueDetails
KGLU1302-SER1321

site_idSWS_FT_FI25
Number of Residues18
DetailsTRANSMEM: Helical; Name=S4 of repeat IV => ECO:0000250|UniProtKB:P07293
ChainResidueDetails
KILE1373-THR1391

site_idSWS_FT_FI26
Number of Residues20
DetailsTRANSMEM: Helical; Name=S5 of repeat IV => ECO:0000250|UniProtKB:P07293
ChainResidueDetails
KPHE1410-LYS1430

site_idSWS_FT_FI27
Number of Residues24
DetailsTRANSMEM: Helical; Name=S6 of repeat IV => ECO:0000250|UniProtKB:P07293
ChainResidueDetails
KILE1500-ILE1524

site_idSWS_FT_FI28
Number of Residues3
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P07293
ChainResidueDetails
KGLU363
KGLU706
KILE1135

site_idSWS_FT_FI29
Number of Residues3
DetailsSITE: Calcium ion selectivity and permeability => ECO:0000269|PubMed:8099908
ChainResidueDetails
KGLU363
KILE1135
KALA1464

site_idSWS_FT_FI30
Number of Residues3
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q01815
ChainResidueDetails
KSER469
KSER808
KSER815

site_idSWS_FT_FI31
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q01815
ChainResidueDetails
KTHR476

site_idSWS_FT_FI32
Number of Residues4
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
KASN153
KASN328
KGLU1436
KSER1487

222415

PDB entries from 2024-07-10

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