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6W8A

K2P2.1 (TREK-1):ML335 complex, 10 mM K+

Functional Information from GO Data
ChainGOidnamespacecontents
A0005267molecular_functionpotassium channel activity
A0016020cellular_componentmembrane
A0071805biological_processpotassium ion transmembrane transport
B0005267molecular_functionpotassium channel activity
B0016020cellular_componentmembrane
B0071805biological_processpotassium ion transmembrane transport
Functional Information from PDB Data
site_idAC1
Number of Residues9
Detailsbinding site for residue K A 401
ChainResidue
AGLY144
APHE145
AGLY253
APHE254
BGLY144
BPHE145
BGLY253
BPHE254
BK402

site_idAC2
Number of Residues10
Detailsbinding site for residue K A 402
ChainResidue
ATHR142
AILE143
ATHR251
AILE252
AK408
BTHR142
BILE143
BTHR251
BILE252
BK402

site_idAC3
Number of Residues14
Detailsbinding site for residue Q6F A 403
ChainResidue
AHIS126
ASER131
APHE134
AGLY137
ATHR138
AILE148
AVAL258
AALA259
AGLY260
AGLY261
AVAL274
ATRP275
AILE278
ACD409

site_idAC4
Number of Residues1
Detailsbinding site for residue 16C A 404
ChainResidue
ATYR57

site_idAC5
Number of Residues5
Detailsbinding site for residue K A 408
ChainResidue
ATHR142
ATHR251
AK402
BTHR142
BTHR251

site_idAC6
Number of Residues2
Detailsbinding site for residue CD A 409
ChainResidue
AASP263
AQ6F403

site_idAC7
Number of Residues1
Detailsbinding site for residue LNK A 410
ChainResidue
ALEU221

site_idAC8
Number of Residues10
Detailsbinding site for residue K B 402
ChainResidue
AILE143
AGLY144
AILE252
AGLY253
AK401
AK402
BILE143
BGLY144
BILE252
BGLY253

site_idAC9
Number of Residues2
Detailsbinding site for residue CD B 403
ChainResidue
BHIS126
BASP263

site_idAD1
Number of Residues4
Detailsbinding site for residue CD B 404
ChainResidue
AGLU309
AHIS313
BGLU309
BHIS313

site_idAD2
Number of Residues1
Detailsbinding site for residue CD B 405
ChainResidue
BASP128

site_idAD3
Number of Residues1
Detailsbinding site for residue R16 B 406
ChainResidue
BALA300

site_idAD4
Number of Residues1
Detailsbinding site for residue R16 B 407
ChainResidue
BILE60

site_idAD5
Number of Residues2
Detailsbinding site for residue R16 B 408
ChainResidue
BILE229
BTRP277

site_idAD6
Number of Residues13
Detailsbinding site for residue Q6F B 409
ChainResidue
BHIS126
BSER131
BPHE134
BGLY137
BTHR138
BPHE145
BILE148
BALA259
BGLY260
BGLY261
BVAL274
BTRP275
BILE278

site_idAD7
Number of Residues1
Detailsbinding site for residue R16 B 410
ChainResidue
BCYS219

site_idAD8
Number of Residues1
Detailsbinding site for residue R16 B 411
ChainResidue
BASP268

site_idAD9
Number of Residues1
Detailsbinding site for residue K B 413
ChainResidue
BASN111

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues160
DetailsTRANSMEM: Helical => ECO:0000255
ChainResidueDetails
AVAL47-ALA67
AILE157-VAL177
AILE208-VAL228
AVAL273-GLY293
BVAL47-ALA67
BILE157-VAL177
BILE208-VAL228
BVAL273-GLY293

site_idSWS_FT_FI2
Number of Residues52
DetailsINTRAMEM: Pore-forming; Name=Pore-forming 1 => ECO:0000255
ChainResidueDetails
ALEU129-GLY155
BLEU129-GLY155

site_idSWS_FT_FI3
Number of Residues58
DetailsTOPO_DOM: Cytoplasmic => ECO:0000255
ChainResidueDetails
AGLY178-ARG207
BGLY178-ARG207

site_idSWS_FT_FI4
Number of Residues60
DetailsINTRAMEM: Pore-forming; Name=Pore-forming 2 => ECO:0000255
ChainResidueDetails
AALA238-ASP268
BALA238-ASP268

site_idSWS_FT_FI5
Number of Residues4
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
ASER95
AALA119
BSER95
BALA119

220113

PDB entries from 2024-05-22

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