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3LNM

F233W mutant of the Kv2.1 paddle-Kv1.2 chimera channel

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
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
A0034705cellular_componentpotassium channel complex
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
A1990002molecular_functionmethylglyoxal reductase (NADPH) (acetol producing) activity
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
C0002244biological_processhematopoietic progenitor cell differentiation
C0004033molecular_functionaldo-keto reductase (NADPH) activity
C0005249molecular_functionvoltage-gated potassium channel activity
C0005515molecular_functionprotein binding
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0005856cellular_componentcytoskeleton
C0005874cellular_componentmicrotubule
C0005886cellular_componentplasma membrane
C0006813biological_processpotassium ion transport
C0008076cellular_componentvoltage-gated potassium channel complex
C0009898cellular_componentcytoplasmic side of plasma membrane
C0014069cellular_componentpostsynaptic density
C0015459molecular_functionpotassium channel regulator activity
C0016020cellular_componentmembrane
C0016491molecular_functionoxidoreductase activity
C0030424cellular_componentaxon
C0034705cellular_componentpotassium channel complex
C0043005cellular_componentneuron projection
C0043194cellular_componentaxon initial segment
C0043679cellular_componentaxon terminus
C0044224cellular_componentjuxtaparanode region of axon
C0044325molecular_functiontransmembrane transporter binding
C0044877molecular_functionprotein-containing complex binding
C0045202cellular_componentsynapse
C0045445biological_processmyoblast differentiation
C0050905biological_processneuromuscular process
C0055085biological_processtransmembrane transport
C0055114biological_processobsolete oxidation-reduction process
C0070995biological_processNADPH oxidation
C0071805biological_processpotassium ion transmembrane transport
C0098839cellular_componentpostsynaptic density membrane
C0098900biological_processregulation of action potential
C0098978cellular_componentglutamatergic synapse
C1901379biological_processregulation of potassium ion transmembrane transport
C1990002molecular_functionmethylglyoxal reductase (NADPH) (acetol producing) activity
C1990031cellular_componentpinceau fiber
C2000008biological_processregulation of protein localization to cell surface
D0005216molecular_functionmonoatomic ion channel activity
D0005249molecular_functionvoltage-gated potassium channel activity
D0006811biological_processmonoatomic ion transport
D0006813biological_processpotassium ion transport
D0008076cellular_componentvoltage-gated potassium channel complex
D0016020cellular_componentmembrane
D0051260biological_processprotein homooligomerization
D0055085biological_processtransmembrane transport
Functional Information from PDB Data
site_idAC1
Number of Residues28
DetailsBINDING SITE FOR RESIDUE NAP A 1001
ChainResidue
AGLY55
AARG189
AGLN214
ATRP243
ASER244
APRO245
ALEU246
AALA247
ACYS248
AGLY249
ALYS254
ATHR56
ASER263
AARG264
ALEU321
AGLY323
ASER325
AGLN329
AGLU332
AASN333
AHOH2036
ATRP57
AGLN63
AASP85
ATYR90
ALYS118
AASN158
ASER188

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE PGW B 601
ChainResidue
BILE328
BPRO358
BPHE361
BTRP362
BLYS384
BSER388
BPGW605

site_idAC3
Number of Residues1
DetailsBINDING SITE FOR RESIDUE PGW B 602
ChainResidue
BHOH2130

site_idAC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE PGW B 605
ChainResidue
BVAL178
BPGW601

site_idAC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE PGW B 606
ChainResidue
BTHR397
BPGW609

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PGW B 608
ChainResidue
BSER307
BLYS308
BGLY309
BARG322
BLEU326
BPHE329

site_idAC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE PGW B 609
ChainResidue
BPHE330
BTHR397
BPGW606

site_idAC8
Number of Residues8
DetailsBINDING SITE FOR RESIDUE PGW B 610
ChainResidue
BILE254
BMET255
BLYS308
BGLN311
BGLY314
BGLN315
BLYS318
BARG415

site_idAC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PGW B 611
ChainResidue
BGLN214
BSER215
BTHR216
BILE231

site_idBC1
Number of Residues1
DetailsBINDING SITE FOR RESIDUE PGW B 612
ChainResidue
BPHE218

site_idBC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE K B 501
ChainResidue
BGLY372
BGLY372
BGLY372
BGLY372
BTYR373
BTYR373
BTYR373
BTYR373

site_idBC3
Number of Residues12
DetailsBINDING SITE FOR RESIDUE K B 502
ChainResidue
BVAL371
BVAL371
BVAL371
BVAL371
BGLY372
BGLY372
BGLY372
BGLY372
BK503
BK503
BK503
BK503

site_idBC4
Number of Residues12
DetailsBINDING SITE FOR RESIDUE K B 503
ChainResidue
BTHR370
BTHR370
BTHR370
BTHR370
BVAL371
BVAL371
BVAL371
BVAL371
BK502
BK502
BK502
BK502

site_idBC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE K B 504
ChainResidue
BTHR370
BTHR370
BTHR370
BTHR370

site_idBC6
Number of Residues30
DetailsBINDING SITE FOR RESIDUE NAP C 1001
ChainResidue
CTHR56
CTRP57
CGLN63
CASP85
CTYR90
CASN158
CSER188
CARG189
CGLN214
CTRP243
CSER244
CPRO245
CLEU246
CALA247
CCYS248
CGLY249
CSER252
CLYS254
CTYR262
CSER263
CARG264
CLEU321
CGLY323
CSER325
CGLN329
CGLU332
CASN333
CHOH2028
CHOH2038
CGLY55

site_idBC7
Number of Residues7
DetailsBINDING SITE FOR RESIDUE PGW D 601
ChainResidue
DPRO358
DPHE361
DTRP362
DVAL365
DILE381
DLYS384
DSER388

site_idBC8
Number of Residues12
DetailsBINDING SITE FOR RESIDUE K D 501
ChainResidue
DGLY372
DGLY372
DGLY372
DGLY372
DTYR373
DTYR373
DTYR373
DTYR373
DK502
DK502
DK502
DK502

site_idBC9
Number of Residues12
DetailsBINDING SITE FOR RESIDUE K D 502
ChainResidue
DVAL371
DVAL371
DVAL371
DVAL371
DGLY372
DGLY372
DGLY372
DGLY372
DK501
DK501
DK501
DK501

site_idCC1
Number of Residues12
DetailsBINDING SITE FOR RESIDUE K D 503
ChainResidue
DTHR370
DTHR370
DTHR370
DTHR370
DVAL371
DVAL371
DVAL371
DVAL371
DK504
DK504
DK504
DK504

site_idCC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE K D 504
ChainResidue
DTHR370
DTHR370
DTHR370
DTHR370
DK503
DK503
DK503
DK503

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues366
DetailsTOPO_DOM: Cytoplasmic => ECO:0000269|PubMed:18004376, ECO:0000269|PubMed:20360102, ECO:0000269|PubMed:20534430
ChainResidueDetails
BMET1-GLY160
BCYS244-ILE254
BSER307-MET321
DMET1-GLY160
DCYS244-ILE254
DSER307-MET321

site_idSWS_FT_FI2
Number of Residues42
DetailsTRANSMEM: Helical; Name=Segment S1 => ECO:0000269|PubMed:18004376, ECO:0000269|PubMed:20360102, ECO:0000269|PubMed:20534430
ChainResidueDetails
BPRO161-LEU182
ALYS254
AARG264
ASER325
AGLN329
AASN333
CTHR56
CTRP57
CGLN63
CASP85
CSER188
DPRO161-LEU182
CGLN214
CTRP243
CSER244
CLEU246
CLYS254
CARG264
CSER325
CGLN329
CASN333
AGLN63
AASP85
ASER188
AGLN214
ATRP243
ASER244
ALEU246

site_idSWS_FT_FI3
Number of Residues76
DetailsTOPO_DOM: Extracellular => ECO:0000269|PubMed:18004376, ECO:0000269|PubMed:20360102, ECO:0000269|PubMed:20534430, ECO:0000305|PubMed:12151401
ChainResidueDetails
BGLU183-PRO221
DGLU183-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
DPHE222-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
DARG322-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
DPHE344-ILE357
DPRO378-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
DPRO358-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
DTHR370-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
DILE385-TYR413

site_idSWS_FT_FI10
Number of Residues162
DetailsTOPO_DOM: Cytoplasmic => ECO:0000269|PubMed:12151401, ECO:0000305
ChainResidueDetails
BHIS414-VAL495
DHIS414-VAL495

site_idSWS_FT_FI11
Number of Residues2
DetailsSITE: Important for normal, slow channel gating => ECO:0000269|PubMed:17766348
ChainResidueDetails
BTHR252
DTHR252

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
DVAL377

site_idSWS_FT_FI13
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P63141
ChainResidueDetails
BTYR425
DTYR425

site_idSWS_FT_FI14
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P63141
ChainResidueDetails
BSER430
DSER430

site_idSWS_FT_FI15
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:18003609, ECO:0007744|PubMed:22673903
ChainResidueDetails
BSER436
DSER436

site_idSWS_FT_FI16
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:22673903
ChainResidueDetails
BSER437
BSER464
DSER437
DSER464

site_idSWS_FT_FI17
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:18003609, ECO:0000269|PubMed:21602278
ChainResidueDetails
BSER445
DSER445

site_idSWS_FT_FI18
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0000305|PubMed:21602278
ChainResidueDetails
BTYR454
DTYR454

site_idSWS_FT_FI19
Number of Residues2
DetailsLIPID: S-palmitoyl cysteine => ECO:0000255
ChainResidueDetails
BCYS244
DCYS244

site_idSWS_FT_FI20
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255, ECO:0000269|PubMed:16770729
ChainResidueDetails
BGLN207
DGLN207

site_idSWS_FT_FI21
Number of Residues26
DetailsTOPO_DOM: Extracellular => ECO:0000250|UniProtKB:P63142
ChainResidueDetails
BGLU274-ARG287
DGLU274-ARG287

222926

PDB entries from 2024-07-24

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