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5MFQ

Crystal structure of the GluK1 ligand-binding domain in complex with kainate and BPAM-344 at 1.90 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 Residues12
Detailsbinding site for residue 2J9 A 901
ChainResidue
APRO532
BTHR535
BLEU783
BLEU791
ATHR535
ASER761
ALYS762
AGLY763
BLYS531
BPRO532
BPHE533
BMET534

site_idAC2
Number of Residues13
Detailsbinding site for residue 2J9 A 902
ChainResidue
ALYS531
APRO532
APHE533
AMET534
ATHR535
ALEU783
ALEU791
BILE519
BPRO532
BTHR535
BSER761
BLYS762
BGLY763

site_idAC3
Number of Residues12
Detailsbinding site for residue KAI A 903
ChainResidue
AGLU441
ATYR489
APRO516
ATHR518
AARG523
AGLY688
ASER689
ATHR690
AGLU738
AHOH1024
AHOH1060
AHOH1077

site_idAC4
Number of Residues4
Detailsbinding site for residue CL A 904
ChainResidue
ALYS531
AHOH1083
BLYS531
BHOH1116

site_idAC5
Number of Residues9
Detailsbinding site for residue GOL A 905
ChainResidue
ALYS488
ATYR489
AGLY490
AALA491
AARG686
AASP687
AHOH1069
AHOH1145
AHOH1167

site_idAC6
Number of Residues6
Detailsbinding site for residue GOL A 906
ChainResidue
AGLU442
ASER721
AASP722
AMET737
ASER741
AHOH1014

site_idAC7
Number of Residues4
Detailsbinding site for residue SO4 A 907
ChainResidue
AHOH1132
BARG448
BSER450
BLYS452

site_idAC8
Number of Residues12
Detailsbinding site for residue KAI B 901
ChainResidue
BGLU441
BTYR489
BPRO516
BTHR518
BARG523
BGLY688
BSER689
BTHR690
BGLU738
BHOH1016
BHOH1056
BHOH1099

site_idAC9
Number of Residues7
Detailsbinding site for residue GOL B 902
ChainResidue
AHOH1085
BARG459
BLYS482
BHOH1006
BHOH1007
BHOH1058
BHOH1235

site_idAD1
Number of Residues5
Detailsbinding site for residue SO4 B 903
ChainResidue
AARG459
ALYS482
AHOH1040
BHOH1066
BHOH1206

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"15710405","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1YCJ","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"15710405","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15721240","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1YCJ","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine; by PKC","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsModified residue: {"description":"Phosphothreonine; by PKC","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

249697

PDB entries from 2026-02-25

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