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5NEB

Structure of GluK1 ligand-binding domain (S1S2) in complex with LM-12b at 2.05 A resolution

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 Residues4
Detailsbinding site for residue SO4 B 301
ChainResidue
BARG31
BVAL53
BLYS54
BLEU55

site_idAC2
Number of Residues2
Detailsbinding site for residue SO4 B 302
ChainResidue
BASP79
BARG81

site_idAC3
Number of Residues6
Detailsbinding site for residue SO4 B 303
ChainResidue
BTRP158
BSER162
BHOH427
BGLY1
BALA2
BLYS147

site_idAC4
Number of Residues3
Detailsbinding site for residue SO4 B 304
ChainResidue
BASP58
BLYS60
BASN71

site_idAC5
Number of Residues5
Detailsbinding site for residue SO4 B 305
ChainResidue
BARG138
BLEU169
BVAL170
BLYS171
BGLU175

site_idAC6
Number of Residues2
Detailsbinding site for residue CL B 306
ChainResidue
BASP100
BPHE101

site_idAC7
Number of Residues2
Detailsbinding site for residue CL B 307
ChainResidue
BASP212
BSER213

site_idAC8
Number of Residues4
Detailsbinding site for residue GOL B 308
ChainResidue
BTHR92
BTYR93
BVAL94
BLYS214

site_idAC9
Number of Residues11
Detailsbinding site for residue 8VE B 309
ChainResidue
BTYR61
BPRO88
BTHR90
BARG95
BGLY140
BSER141
BTHR142
BGLU190
BSER193
BHOH413
BHOH423

site_idAD1
Number of Residues4
Detailsbinding site for residue ACT B 310
ChainResidue
BARG20
BASP38
BLYS41
BLYS249

site_idAD2
Number of Residues3
Detailsbinding site for residue SO4 A 301
ChainResidue
AGLY209
ALEU210
BHIS244

site_idAD3
Number of Residues4
Detailsbinding site for residue SO4 A 302
ChainResidue
AHIS244
AHOH475
BGLY209
BLEU210

site_idAD4
Number of Residues4
Detailsbinding site for residue SO4 A 303
ChainResidue
AARG31
AVAL53
ALYS54
ALEU55

site_idAD5
Number of Residues3
Detailsbinding site for residue CL A 304
ChainResidue
APHE101
AARG227
AHOH455

site_idAD6
Number of Residues1
Detailsbinding site for residue CL A 305
ChainResidue
ASER213

site_idAD7
Number of Residues7
Detailsbinding site for residue GOL A 306
ChainResidue
ATHR92
ATYR93
AVAL94
ALYS214
AHOH438
AHOH444
AHOH469

site_idAD8
Number of Residues14
Detailsbinding site for residue 8VE A 307
ChainResidue
ATYR61
APRO88
ALEU89
ATHR90
AARG95
AGLY140
ASER141
ATHR142
AGLU190
ASER193
ATYR216
AHOH421
AHOH427
AHOH434

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:15710405, ECO:0007744|PDB:1YCJ
ChainResidueDetails
BLYS103
BPHE105
BLYS156
BMET157
ALYS103
APHE105
ALYS156
AMET157

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:15710405, ECO:0000269|PubMed:15721240, ECO:0007744|PDB:1YCJ
ChainResidueDetails
BILE110
BTHR205
AILE110
ATHR205

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Phosphoserine; by PKC => ECO:0000255
ChainResidueDetails
BILE177
AILE177

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphothreonine; by PKC => ECO:0000255
ChainResidueDetails
BSER213
ASER213

site_idSWS_FT_FI5
Number of Residues6
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
BILE11
BMET18
BVAL218
AILE11
AMET18
AVAL218

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PDB entries from 2024-07-17

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