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6JMV

Crystal structure of the GluK3 ligand binding domain complex with SYM and zinc

Functional Information from GO Data
ChainGOidnamespacecontents
A0015276molecular_functionligand-gated monoatomic ion channel activity
A0016020cellular_componentmembrane
B0015276molecular_functionligand-gated monoatomic ion channel activity
B0016020cellular_componentmembrane
Functional Information from PDB Data
site_idAC1
Number of Residues12
Detailsbinding site for residue SYM A 301
ChainResidue
ATYR61
AHOH421
AHOH441
AHOH492
APRO88
ATHR90
AARG95
AGLY140
AALA141
ATHR142
AASN172
AGLU189

site_idAC2
Number of Residues2
Detailsbinding site for residue CL A 302
ChainResidue
AARG31
ALEU55

site_idAC3
Number of Residues4
Detailsbinding site for residue ZN A 303
ChainResidue
AGLU194
AHIS243
ALYS246
AGLU247

site_idAC4
Number of Residues6
Detailsbinding site for residue GOL A 304
ChainResidue
AGLU13
AGLU14
AASN172
AGLU173
AILE176
ATHR192

site_idAC5
Number of Residues3
Detailsbinding site for residue ACT A 305
ChainResidue
ASER2
AARG4
BHIS93

site_idAC6
Number of Residues4
Detailsbinding site for residue ACT A 306
ChainResidue
AILE91
ATHR92
AHIS93
AHOH422

site_idAC7
Number of Residues4
Detailsbinding site for residue ZN A 307
ChainResidue
AHIS80
AHOH557
BHIS93
BHOH484

site_idAC8
Number of Residues3
Detailsbinding site for residue ACT A 308
ChainResidue
ALYS228
BGLY222
BACT310

site_idAC9
Number of Residues4
Detailsbinding site for residue ZN B 301
ChainResidue
AHIS93
AGLU96
BASP240
BHIS243

site_idAD1
Number of Residues11
Detailsbinding site for residue SYM B 302
ChainResidue
BTYR61
BPRO88
BTHR90
BARG95
BGLY140
BALA141
BTHR142
BGLU189
BHOH419
BHOH423
BHOH476

site_idAD2
Number of Residues4
Detailsbinding site for residue ZN B 303
ChainResidue
BHIS80
BHIS80
BHOH458
BHOH458

site_idAD3
Number of Residues3
Detailsbinding site for residue CL B 304
ChainResidue
BARG31
BARG54
BLEU55

site_idAD4
Number of Residues2
Detailsbinding site for residue CL B 305
ChainResidue
BASP58
BLYS60

site_idAD5
Number of Residues6
Detailsbinding site for residue GOL B 306
ChainResidue
BLYS60
BTYR61
BGLY62
BALA63
BASN71
BASP139

site_idAD6
Number of Residues7
Detailsbinding site for residue GOL B 307
ChainResidue
AHIS93
BGLN237
BASP240
BLEU242
BHIS243
BHOH401
BHOH494

site_idAD7
Number of Residues9
Detailsbinding site for residue GOL B 308
ChainResidue
BGLU14
BSER22
BASP23
BARG24
BTHR25
BARG199
BCL313
BHOH402
BHOH425

site_idAD8
Number of Residues5
Detailsbinding site for residue GOL B 309
ChainResidue
BGLU13
BGLU14
BASN172
BGLU173
BTHR192

site_idAD9
Number of Residues5
Detailsbinding site for residue ACT B 310
ChainResidue
AGLY1
ASER2
AACT308
BASP100
BARG226

site_idAE1
Number of Residues3
Detailsbinding site for residue ACT B 311
ChainResidue
BSER190
BGLU194
BGLN205

site_idAE2
Number of Residues7
Detailsbinding site for residue ACT B 312
ChainResidue
BILE46
BGLN235
BGLN235
BGLU239
BLYS241
BGLU42
BHIS45

site_idAE3
Number of Residues3
Detailsbinding site for residue CL B 313
ChainResidue
BGLU14
BLYS21
BGOL308

site_idAE4
Number of Residues1
Detailsbinding site for residue NA B 314
ChainResidue
BGLU194

site_idAE5
Number of Residues3
Detailsbinding site for residue NA B 315
ChainResidue
AASN3
AHOH537
BASP227

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:21907808
ChainResidueDetails
ATHR90
AARG95
AGLU189
BTHR90
BARG95
BGLU189

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING:
ChainResidueDetails
AGLY140
BGLY140

site_idSWS_FT_FI3
Number of Residues4
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN3
AASN202
BASN3
BASN202

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PDB entries from 2024-06-12

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