Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

4QF9

Structure of GluK1 ligand-binding domain (S1S2) in complex with (S)-2-amino-4-(2,3-dioxo-1,2,3,4-tetrahydroquinoxalin-6-yl)butanoic acid at 2.28 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
C0015276molecular_functionligand-gated monoatomic ion channel activity
C0016020cellular_componentmembrane
Functional Information from PDB Data
site_idAC1
Number of Residues10
DetailsBINDING SITE FOR RESIDUE 35K A 301
ChainResidue
ATYR16
AHOH417
ATYR61
APRO88
ALEU89
ATHR90
AARG95
ATHR192
ASER193
ATYR216

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 302
ChainResidue
AGLY140
ASER141
ATHR142
AGLU190
AHOH429
AHOH453

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PG4 A 303
ChainResidue
AARG31
ALYS54
ALEU55
AGLU133
ASER167
AARG179

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL A 304
ChainResidue
ALYS171
ALYS171
AASN172
AASN172

site_idAC5
Number of Residues14
DetailsBINDING SITE FOR RESIDUE 35K B 301
ChainResidue
BGLU13
BTYR16
BTYR61
BPRO88
BLEU89
BTHR90
BARG95
BTHR192
BSER193
BTYR216
BHOH425
BHOH448
BHOH449
BHOH472

site_idAC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 B 302
ChainResidue
BSER141
BTHR142
BGLU190
BHOH413
BHOH462
BHOH463
BHOH482

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 B 303
ChainResidue
AILE151
ASER152
BLYS229
BHOH429

site_idAC8
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL B 304
ChainResidue
BASP212
BHIS244
BHOH456

site_idAC9
Number of Residues2
DetailsBINDING SITE FOR RESIDUE GOL B 305
ChainResidue
BARG31
BLEU55

site_idBC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL B 306
ChainResidue
BARG179
BHOH438
CARG31
CHOH441

site_idBC2
Number of Residues13
DetailsBINDING SITE FOR RESIDUE PG4 B 307
ChainResidue
BGLU96
BGLU96
BPHE101
BPHE101
BSER102
BLYS103
BLYS103
BARG227
BARG227
BASP228
BASP228
BTHR231
BTHR231

site_idBC3
Number of Residues9
DetailsBINDING SITE FOR RESIDUE 35K C 301
ChainResidue
CGLU13
CGLU14
CTYR16
CTYR61
CPRO88
CTHR90
CARG95
CTHR192
CTYR216

site_idBC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 C 302
ChainResidue
CVAL137
CGLY140
CSER141
CTHR142
CMET189
CGLU190

site_idBC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ACT C 303
ChainResidue
ASER213
CHIS244
CHOH432

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBINDING:
ChainResidueDetails
APRO88
ASER141
BPRO88
BSER141
CPRO88
CSER141

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:15710405, ECO:0000269|PubMed:15721240
ChainResidueDetails
BGLU190
CARG95
CGLU190
AARG95
AGLU190
BARG95

site_idSWS_FT_FI3
Number of Residues3
DetailsMOD_RES: Phosphoserine; by PKC => ECO:0000255
ChainResidueDetails
ASER162
BSER162
CSER162

site_idSWS_FT_FI4
Number of Residues3
DetailsMOD_RES: Phosphothreonine; by PKC => ECO:0000255
ChainResidueDetails
ATHR198
BTHR198
CTHR198

site_idSWS_FT_FI5
Number of Residues6
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN3
AASN203
BASN3
BASN203
CASN3
CASN203

219869

PDB entries from 2024-05-15

PDB statisticsPDBj update infoContact PDBjnumon