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7VFU

Human N-type voltage gated calcium channel CaV2.2-alpha2/delta1-beta1 complex, bound to ziconotide

Functional Information from GO Data
ChainGOidnamespacecontents
A0001540molecular_functionamyloid-beta binding
A0005216molecular_functionmonoatomic ion channel activity
A0005245molecular_functionvoltage-gated calcium channel activity
A0005262molecular_functioncalcium channel activity
A0005509molecular_functioncalcium ion binding
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005886cellular_componentplasma membrane
A0005891cellular_componentvoltage-gated calcium channel complex
A0006811biological_processmonoatomic ion transport
A0006816biological_processcalcium ion transport
A0007268biological_processchemical synaptic transmission
A0008331molecular_functionhigh voltage-gated calcium channel activity
A0016020cellular_componentmembrane
A0034702cellular_componentmonoatomic ion channel complex
A0043025cellular_componentneuronal cell body
A0045202cellular_componentsynapse
A0046872molecular_functionmetal ion binding
A0050804biological_processmodulation of chemical synaptic transmission
A0055085biological_processtransmembrane transport
A0070588biological_processcalcium ion transmembrane transport
A0098703biological_processcalcium ion import across plasma membrane
A1904645biological_processresponse to amyloid-beta
D0005245molecular_functionvoltage-gated calcium channel activity
D0005246molecular_functioncalcium channel regulator activity
D0005262molecular_functioncalcium channel activity
D0005515molecular_functionprotein binding
D0005886cellular_componentplasma membrane
D0005891cellular_componentvoltage-gated calcium channel complex
D0007268biological_processchemical synaptic transmission
D0007528biological_processneuromuscular junction development
D0008331molecular_functionhigh voltage-gated calcium channel activity
D0030315cellular_componentT-tubule
D0034702cellular_componentmonoatomic ion channel complex
D0042383cellular_componentsarcolemma
D0045202cellular_componentsynapse
D0045933biological_processpositive regulation of muscle contraction
D0070588biological_processcalcium ion transmembrane transport
D1902514biological_processregulation of calcium ion transmembrane transport via high voltage-gated calcium channel
D1904646biological_processcellular response to amyloid-beta
D1990454cellular_componentL-type voltage-gated calcium channel complex
E0005576cellular_componentextracellular region
E0008200molecular_functionion channel inhibitor activity
Functional Information from PROSITE/UniProt
site_idPS60004
Number of Residues25
DetailsOMEGA_CONOTOXIN Omega-conotoxin family signature. CKgkGaKCSrl...MYdCCTg.SCr..SGKC
ChainResidueDetails
ECYS1-CYS25

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1048
DetailsTOPO_DOM: Extracellular => ECO:0000255
ChainResidueDetails
BGLU25-GLY1073
AILE1417-PRO1471
AALA1524-ASP1533
ATYR1583-TYR1601
AMET1708-CYS2339
DSER47
DSER73
DSER193
EARG21
ALYS587-ASN604
AASP710-TYR1151
AASP1204-ASP1217
APRO1266-LEU1283

site_idSWS_FT_FI2
Number of Residues20
DetailsTRANSMEM: Helical => ECO:0000255
ChainResidueDetails
BVAL1074-LEU1094
DSER547

site_idSWS_FT_FI3
Number of Residues8
DetailsTOPO_DOM: Cytoplasmic => ECO:0000255
ChainResidueDetails
BVAL1095-LEU1103
ALYS1491-GLU1498
AALA1556-ASN1563
AGLY1622-PHE1683
AGLY183-ASP187
ATYR245-TRP331
AVAL502-THR511
ALYS567-GLY573
APHE631-GLY682
AASP1171-PRO1178
ASER1239-ILE1244
APHE1304-MET1390

site_idSWS_FT_FI4
Number of Residues3
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
BASP259
BSER261
BSER263

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P54290
ChainResidueDetails
BSER119

site_idSWS_FT_FI6
Number of Residues7
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:34234349, ECO:0007744|PDB:7MIX, ECO:0007744|PDB:7MIY
ChainResidueDetails
BASN92
BASN184
BASN348
BASN468
BASN613
BASN781
BASN895

site_idSWS_FT_FI7
Number of Residues9
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
BASN136
BASN324
BASN475
BASN604
BASN675
BASN824
BASN888
BASN985
BASN998

site_idSWS_FT_FI8
Number of Residues24
DetailsTRANSMEM: Helical; Name=S6 of repeat I => ECO:0000269|PubMed:34234349, ECO:0007744|PDB:7MIX, ECO:0007744|PDB:7MIY
ChainResidueDetails
AASN332-SER356

site_idSWS_FT_FI9
Number of Residues18
DetailsTRANSMEM: Helical; Name=S1 of repeat II => ECO:0000269|PubMed:34234349, ECO:0007744|PDB:7MIX, ECO:0007744|PDB:7MIY
ChainResidueDetails
ASER483-MET501

site_idSWS_FT_FI10
Number of Residues22
DetailsTRANSMEM: Helical; Name=S2 of repeat II => ECO:0000269|PubMed:34234349, ECO:0007744|PDB:7MIX, ECO:0007744|PDB:7MIY
ChainResidueDetails
ATHR512-TYR534

site_idSWS_FT_FI11
Number of Residues21
DetailsTRANSMEM: Helical; Name=S3 of repeat II => ECO:0000269|PubMed:34234349, ECO:0007744|PDB:7MIX, ECO:0007744|PDB:7MIY
ChainResidueDetails
ASER545-ILE566

site_idSWS_FT_FI12
Number of Residues12
DetailsTRANSMEM: Helical; Name=S4 of repeat II => ECO:0000269|PubMed:34234349, ECO:0007744|PDB:7MIX, ECO:0007744|PDB:7MIY
ChainResidueDetails
AILE574-PHE586

site_idSWS_FT_FI13
Number of Residues25
DetailsTRANSMEM: Helical; Name=S5 of repeat II => ECO:0000269|PubMed:34234349, ECO:0007744|PDB:7MIX, ECO:0007744|PDB:7MIY
ChainResidueDetails
ASER605-LEU630

site_idSWS_FT_FI14
Number of Residues26
DetailsTRANSMEM: Helical; Name=S6 of repeat II => ECO:0000269|PubMed:34234349, ECO:0007744|PDB:7MIX, ECO:0007744|PDB:7MIY
ChainResidueDetails
AMET683-VAL709

site_idSWS_FT_FI15
Number of Residues18
DetailsTRANSMEM: Helical; Name=S1 of repeat III => ECO:0000269|PubMed:34234349, ECO:0007744|PDB:7MIX, ECO:0007744|PDB:7MIY
ChainResidueDetails
APHE1152-GLU1170

site_idSWS_FT_FI16
Number of Residues24
DetailsTRANSMEM: Helical; Name=S2 of repeat III => ECO:0000269|PubMed:34234349, ECO:0007744|PDB:7MIX, ECO:0007744|PDB:7MIY
ChainResidueDetails
AARG1179-ILE1203

site_idSWS_FT_FI17
Number of Residues20
DetailsTRANSMEM: Helical; Name=S3 of repeat III => ECO:0000269|PubMed:34234349, ECO:0007744|PDB:7MIX, ECO:0007744|PDB:7MIY
ChainResidueDetails
ALEU1218-GLY1238

site_idSWS_FT_FI18
Number of Residues20
DetailsTRANSMEM: Helical; Name=S4 of repeat III => ECO:0000269|PubMed:34234349, ECO:0007744|PDB:7MIX, ECO:0007744|PDB:7MIY
ChainResidueDetails
AASN1245-LEU1265

site_idSWS_FT_FI19
Number of Residues19
DetailsTRANSMEM: Helical; Name=S5 of repeat III => ECO:0000269|PubMed:34234349, ECO:0007744|PDB:7MIX, ECO:0007744|PDB:7MIY
ChainResidueDetails
AASN1284-LEU1303

site_idSWS_FT_FI20
Number of Residues25
DetailsTRANSMEM: Helical; Name=S6 of repeat III => ECO:0000269|PubMed:34234349, ECO:0007744|PDB:7MIX, ECO:0007744|PDB:7MIY
ChainResidueDetails
AGLU1391-ILE1416

site_idSWS_FT_FI21
Number of Residues18
DetailsTRANSMEM: Helical; Name=S1 of repeat IV => ECO:0000269|PubMed:34234349, ECO:0007744|PDB:7MIX, ECO:0007744|PDB:7MIY
ChainResidueDetails
APRO1472-MET1490

site_idSWS_FT_FI22
Number of Residues24
DetailsTRANSMEM: Helical; Name=S2 of repeat IV => ECO:0000269|PubMed:34234349, ECO:0007744|PDB:7MIX, ECO:0007744|PDB:7MIY
ChainResidueDetails
ATYR1499-ILE1523

site_idSWS_FT_FI23
Number of Residues21
DetailsTRANSMEM: Helical; Name=S3 of repeat IV => ECO:0000269|PubMed:34234349, ECO:0007744|PDB:7MIX, ECO:0007744|PDB:7MIY
ChainResidueDetails
AALA1534-ILE1555

site_idSWS_FT_FI24
Number of Residues18
DetailsTRANSMEM: Helical; Name=S4 of repeat IV => ECO:0000269|PubMed:34234349, ECO:0007744|PDB:7MIX, ECO:0007744|PDB:7MIY
ChainResidueDetails
ALEU1564-GLY1582

site_idSWS_FT_FI25
Number of Residues19
DetailsTRANSMEM: Helical; Name=S5 of repeat IV => ECO:0000269|PubMed:34234349, ECO:0007744|PDB:7MIX, ECO:0007744|PDB:7MIY
ChainResidueDetails
AVAL1602-PHE1621

site_idSWS_FT_FI26
Number of Residues23
DetailsTRANSMEM: Helical; Name=S6 of repeat IV => ECO:0000269|PubMed:34234349, ECO:0007744|PDB:7MIX, ECO:0007744|PDB:7MIY
ChainResidueDetails
AALA1684-ILE1707

site_idSWS_FT_FI27
Number of Residues1
DetailsBINDING: BINDING => ECO:0000255
ChainResidueDetails
AALA451

site_idSWS_FT_FI28
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:34234349, ECO:0007744|PDB:7MIX, ECO:0007744|PDB:7MIY
ChainResidueDetails
ASER544
AARG584
ALYS587

site_idSWS_FT_FI29
Number of Residues3
DetailsBINDING: BINDING => ECO:0000305
ChainResidueDetails
AASP1737
AARG1743
AASP1748

site_idSWS_FT_FI30
Number of Residues1
DetailsMOD_RES: Omega-N-methylarginine => ECO:0000250|UniProtKB:O55017
ChainResidueDetails
AARG22

site_idSWS_FT_FI31
Number of Residues9
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:O55017
ChainResidueDetails
ASER411
ASER745
ASER748
ASER783
ASER1069
ASER2066
ASER2224
ASER2233
ASER2256

site_idSWS_FT_FI32
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:34234349, ECO:0007744|PDB:7MIX, ECO:0007744|PDB:7MIY
ChainResidueDetails
AASN256

site_idSWS_FT_FI33
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN1563
AASN1675

226707

PDB entries from 2024-10-30

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