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4JTC

Crystal structure of Kv1.2-2.1 paddle chimera channel in complex with Charybdotoxin in Cs+

Functional Information from GO Data
ChainGOidnamespacecontents
A0002244biological_processhematopoietic progenitor cell differentiation
A0004033molecular_functionaldo-keto reductase (NADPH) activity
A0005249molecular_functionvoltage-gated potassium channel activity
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005856cellular_componentcytoskeleton
A0005874cellular_componentmicrotubule
A0005886cellular_componentplasma membrane
A0006811biological_processmonoatomic ion transport
A0006813biological_processpotassium ion transport
A0008076cellular_componentvoltage-gated potassium channel complex
A0009898cellular_componentcytoplasmic side of plasma membrane
A0014069cellular_componentpostsynaptic density
A0015459molecular_functionpotassium channel regulator activity
A0016020cellular_componentmembrane
A0016491molecular_functionoxidoreductase activity
A0030424cellular_componentaxon
A0031234cellular_componentextrinsic component of cytoplasmic side of plasma membrane
A0034220biological_processmonoatomic ion transmembrane transport
A0034702cellular_componentmonoatomic ion channel complex
A0034705cellular_componentpotassium channel complex
A0042995cellular_componentcell projection
A0043005cellular_componentneuron projection
A0043194cellular_componentaxon initial segment
A0043679cellular_componentaxon terminus
A0044224cellular_componentjuxtaparanode region of axon
A0044325molecular_functiontransmembrane transporter binding
A0044877molecular_functionprotein-containing complex binding
A0045202cellular_componentsynapse
A0045445biological_processmyoblast differentiation
A0050905biological_processneuromuscular process
A0055085biological_processtransmembrane transport
A0055114biological_processobsolete oxidation-reduction process
A0070995biological_processNADPH oxidation
A0071805biological_processpotassium ion transmembrane transport
A0098839cellular_componentpostsynaptic density membrane
A0098900biological_processregulation of action potential
A0098978cellular_componentglutamatergic synapse
A1901379biological_processregulation of potassium ion transmembrane transport
A1990031cellular_componentpinceau fiber
A2000008biological_processregulation of protein localization to cell surface
B0005216molecular_functionmonoatomic ion channel activity
B0005249molecular_functionvoltage-gated potassium channel activity
B0006811biological_processmonoatomic ion transport
B0006813biological_processpotassium ion transport
B0008076cellular_componentvoltage-gated potassium channel complex
B0016020cellular_componentmembrane
B0051260biological_processprotein homooligomerization
B0055085biological_processtransmembrane transport
G0002244biological_processhematopoietic progenitor cell differentiation
G0004033molecular_functionaldo-keto reductase (NADPH) activity
G0005249molecular_functionvoltage-gated potassium channel activity
G0005515molecular_functionprotein binding
G0005737cellular_componentcytoplasm
G0005829cellular_componentcytosol
G0005856cellular_componentcytoskeleton
G0005874cellular_componentmicrotubule
G0005886cellular_componentplasma membrane
G0006811biological_processmonoatomic ion transport
G0006813biological_processpotassium ion transport
G0008076cellular_componentvoltage-gated potassium channel complex
G0009898cellular_componentcytoplasmic side of plasma membrane
G0014069cellular_componentpostsynaptic density
G0015459molecular_functionpotassium channel regulator activity
G0016020cellular_componentmembrane
G0016491molecular_functionoxidoreductase activity
G0030424cellular_componentaxon
G0031234cellular_componentextrinsic component of cytoplasmic side of plasma membrane
G0034220biological_processmonoatomic ion transmembrane transport
G0034702cellular_componentmonoatomic ion channel complex
G0034705cellular_componentpotassium channel complex
G0042995cellular_componentcell projection
G0043005cellular_componentneuron projection
G0043194cellular_componentaxon initial segment
G0043679cellular_componentaxon terminus
G0044224cellular_componentjuxtaparanode region of axon
G0044325molecular_functiontransmembrane transporter binding
G0044877molecular_functionprotein-containing complex binding
G0045202cellular_componentsynapse
G0045445biological_processmyoblast differentiation
G0050905biological_processneuromuscular process
G0055085biological_processtransmembrane transport
G0055114biological_processobsolete oxidation-reduction process
G0070995biological_processNADPH oxidation
G0071805biological_processpotassium ion transmembrane transport
G0098839cellular_componentpostsynaptic density membrane
G0098900biological_processregulation of action potential
G0098978cellular_componentglutamatergic synapse
G1901379biological_processregulation of potassium ion transmembrane transport
G1990031cellular_componentpinceau fiber
G2000008biological_processregulation of protein localization to cell surface
H0005216molecular_functionmonoatomic ion channel activity
H0005249molecular_functionvoltage-gated potassium channel activity
H0006811biological_processmonoatomic ion transport
H0006813biological_processpotassium ion transport
H0008076cellular_componentvoltage-gated potassium channel complex
H0016020cellular_componentmembrane
H0051260biological_processprotein homooligomerization
H0055085biological_processtransmembrane transport
Y0005576cellular_componentextracellular region
Y0008200molecular_functionion channel inhibitor activity
Y0015459molecular_functionpotassium channel regulator activity
Y0031640biological_processkilling of cells of another organism
Y0035821biological_processmodulation of process of another organism
Y0042742biological_processdefense response to bacterium
Y0050832biological_processdefense response to fungus
Y0090729molecular_functiontoxin activity
Y0099106molecular_functionion channel regulator activity
Functional Information from PDB Data
site_idAC1
Number of Residues26
DetailsBINDING SITE FOR RESIDUE NAP A 1001
ChainResidue
AGLY55
AGLN214
ATRP243
ASER244
APRO245
ALEU246
ACYS248
AGLY249
ALYS254
ATYR262
ASER263
ATHR56
AARG264
ALEU322
AGLY323
ASER325
AGLN329
AGLU332
AASN333
ATRP57
AGLN63
AASP85
ATYR90
ALYS118
ASER188
AARG189

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE CS B 501
ChainResidue
BGLY372
BGLY372
BGLY372
BGLY372
BTYR373
BTYR373
BTYR373
BTYR373

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CS B 502
ChainResidue
BVAL371
BVAL371
BVAL371
BVAL371

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CS B 503
ChainResidue
BTHR370
BTHR370
BTHR370
BTHR370

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE PGW B 504
ChainResidue
BILE328
BPRO358
BPHE361
BILE381
BLYS384
BSER388
BPGW509

site_idAC6
Number of Residues2
DetailsBINDING SITE FOR RESIDUE PGW B 505
ChainResidue
BPGW506
BPGW507

site_idAC7
Number of Residues1
DetailsBINDING SITE FOR RESIDUE PGW B 506
ChainResidue
BPGW505

site_idAC8
Number of Residues1
DetailsBINDING SITE FOR RESIDUE PGW B 507
ChainResidue
BPGW505

site_idAC9
Number of Residues2
DetailsBINDING SITE FOR RESIDUE PGW B 509
ChainResidue
BVAL178
BPGW504

site_idBC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PGW B 510
ChainResidue
BLEU313
BILE328
BALA393
BTHR397
BPGW511
BPGW515

site_idBC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE PGW B 511
ChainResidue
BMET321
BPGW510

site_idBC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE PGW B 512
ChainResidue
BILE187
BPHE188

site_idBC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE PGW B 513
ChainResidue
BPRO221
BPHE222

site_idBC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE PGW B 514
ChainResidue
BHIS306
BSER307
BLYS308
BARG322
BGLY325
BLEU326
BPHE329

site_idBC6
Number of Residues1
DetailsBINDING SITE FOR RESIDUE PGW B 515
ChainResidue
BPGW510

site_idBC7
Number of Residues8
DetailsBINDING SITE FOR RESIDUE PGW B 516
ChainResidue
BPHE301
BLEU310
BGLN311
BGLY314
BGLN315
BLYS318
BARG415
BGLU416

site_idBC8
Number of Residues2
DetailsBINDING SITE FOR RESIDUE PGW B 518
ChainResidue
BILE257
BMET295

site_idBC9
Number of Residues30
DetailsBINDING SITE FOR RESIDUE NAP G 1001
ChainResidue
GLEU246
GALA247
GCYS248
GGLY249
GSER252
GLYS254
GTYR262
GSER263
GARG264
GPRO304
GLEU322
GGLY323
GSER325
GGLN329
GGLU332
GASN333
GGLY55
GTHR56
GTRP57
GGLN63
GASP85
GTYR90
GLYS118
GASN158
GSER188
GARG189
GGLN214
GTRP243
GSER244
GPRO245

site_idCC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CS H 501
ChainResidue
HGLY372
HGLY372
HGLY372
HGLY372

site_idCC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CS H 502
ChainResidue
HTHR370
HTHR370
HTHR370
HTHR370

site_idCC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CS H 503
ChainResidue
HTHR370
HTHR370
HTHR370
HTHR370

site_idCC4
Number of Residues8
DetailsBINDING SITE FOR RESIDUE PGW H 504
ChainResidue
HPRO358
HASP359
HPHE361
HTRP362
HVAL365
HILE381
HLYS384
HSER388

Functional Information from PROSITE/UniProt
site_idPS01138
Number of Residues23
DetailsSCORP_SHORT_TOXIN Scorpion short toxins signature. CwsvCqrlhntsr.GKCMnkkCrC
ChainResidueDetails
YCYS13-CYS35

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsSITE: Basic residue of the functional dyad => ECO:0000250
ChainResidueDetails
YLYS27
BCYS244-ILE254
BSER307-MET321
HMET1-GLY160
HCYS244-ILE254
HSER307-MET321

site_idSWS_FT_FI2
Number of Residues1
DetailsSITE: Aromatic residue of the functional dyad => ECO:0000250
ChainResidueDetails
YTYR36
ALYS254
AARG264
ASER325
AGLN329
AASN333
GTHR56
GTRP57
GGLN63
GASP85
GSER188
HPRO161-LEU182
GGLN214
GTRP243
GSER244
GLEU246
GLYS254
GARG264
GSER325
GGLN329
GASN333
AGLN63
AASP85
ASER188
AGLN214
ATRP243
ASER244
ALEU246

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Pyrrolidone carboxylic acid => ECO:0000269|PubMed:2453055, ECO:0000269|PubMed:2482078
ChainResidueDetails
YPCA1
HGLU183-PRO221

site_idSWS_FT_FI4
Number of Residues42
DetailsTRANSMEM: Helical; Name=Segment S2 => ECO:0000269|PubMed:18004376, ECO:0000269|PubMed:20360102, ECO:0000269|PubMed:20534430
ChainResidueDetails
BPHE222-ALA243
HPHE222-ALA243

site_idSWS_FT_FI5
Number of Residues42
DetailsTRANSMEM: Helical; Name=Segment S5 => ECO:0000269|PubMed:18004376, ECO:0000269|PubMed:20360102, ECO:0000269|PubMed:20534430
ChainResidueDetails
BARG322-TYR343
HARG322-TYR343

site_idSWS_FT_FI6
Number of Residues38
DetailsTOPO_DOM: Extracellular => ECO:0000269|PubMed:18004376, ECO:0000269|PubMed:20360102, ECO:0000269|PubMed:20534430
ChainResidueDetails
BPHE344-ILE357
BPRO378-LYS384
HPHE344-ILE357
HPRO378-LYS384

site_idSWS_FT_FI7
Number of Residues22
DetailsINTRAMEM: Helical; Name=Pore helix => ECO:0000269|PubMed:18004376, ECO:0000269|PubMed:20360102, ECO:0000269|PubMed:20534430
ChainResidueDetails
BPRO358-THR369
HPRO358-THR369

site_idSWS_FT_FI8
Number of Residues14
DetailsINTRAMEM: INTRAMEM => ECO:0000269|PubMed:18004376, ECO:0000269|PubMed:20360102, ECO:0000269|PubMed:20534430
ChainResidueDetails
BTHR370-VAL377
HTHR370-VAL377

site_idSWS_FT_FI9
Number of Residues56
DetailsTRANSMEM: Helical; Name=Segment S6 => ECO:0000269|PubMed:18004376, ECO:0000269|PubMed:20360102, ECO:0000269|PubMed:20534430
ChainResidueDetails
BILE385-TYR413
HILE385-TYR413

site_idSWS_FT_FI10
Number of Residues162
DetailsTOPO_DOM: Cytoplasmic => ECO:0000269|PubMed:12151401, ECO:0000305
ChainResidueDetails
BHIS414-VAL495
HHIS414-VAL495

site_idSWS_FT_FI11
Number of Residues2
DetailsSITE: Important for normal, slow channel gating => ECO:0000269|PubMed:17766348
ChainResidueDetails
BTHR252
HTHR252

site_idSWS_FT_FI12
Number of Residues2
DetailsSITE: Important for binding with the scorpion mesomartoxin; when the scorpion mesomartoxin-rKv1.2/KCNA2 interaction is modeled, this residue is close to the 'Y-57' residue of the toxin => ECO:0000305|PubMed:25514171
ChainResidueDetails
BVAL377
HVAL377

site_idSWS_FT_FI13
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P63141
ChainResidueDetails
BTYR425
HTYR425

site_idSWS_FT_FI14
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P63141
ChainResidueDetails
BSER430
HSER430

site_idSWS_FT_FI15
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:18003609, ECO:0007744|PubMed:22673903
ChainResidueDetails
BSER436
HSER436

site_idSWS_FT_FI16
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:22673903
ChainResidueDetails
BSER437
BSER464
HSER437
HSER464

site_idSWS_FT_FI17
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:18003609, ECO:0000269|PubMed:21602278
ChainResidueDetails
BSER445
HSER445

site_idSWS_FT_FI18
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0000305|PubMed:21602278
ChainResidueDetails
BTYR454
HTYR454

site_idSWS_FT_FI19
Number of Residues2
DetailsLIPID: S-palmitoyl cysteine => ECO:0000255
ChainResidueDetails
BCYS244
HCYS244

site_idSWS_FT_FI20
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255, ECO:0000269|PubMed:16770729
ChainResidueDetails
BGLN207
HGLN207

site_idSWS_FT_FI21
Number of Residues26
DetailsTOPO_DOM: Extracellular => ECO:0000250|UniProtKB:P63142
ChainResidueDetails
BGLU274-ARG287
HGLU274-ARG287

218853

PDB entries from 2024-04-24

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