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3FVN

Crystal structure of the human glutamate receptor, GluR5, ligand-binding core in complex with 9-deoxy-neodysiherbaine A in space group P1

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 Residues9
DetailsBINDING SITE FOR RESIDUE GOL A 3968
ChainResidue
AHOH293
ATHR505
ATHR677
APHE678
ALYS747
BHOH4
BHOH23
BHOH43
BHOH56

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL A 3971
ChainResidue
AHOH248
AHOH262
AHOH264
APRO517
ASER746
AGLY748
BTHR520
BGLN771

site_idAC3
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL A 3973
ChainResidue
AHOH246
ALYS516
AARG760
ATHR764
BHOH195
BPHE514
BLYS516
BARG760
BTHR764

site_idAC4
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL A 3976
ChainResidue
AHOH266
ALEU468
AVAL469
APRO470
AGLY472
BHOH26
BHOH85
BARG704

site_idAC5
Number of Residues19
DetailsBINDING SITE FOR RESIDUE 9DX A 1
ChainResidue
AHOH380
AGLU426
ATYR474
APRO501
ALEU502
ATHR503
AARG508
AVAL670
AGLY673
ASER674
ATHR675
ASER706
AMET722
AGLU723
ASER726
ATYR749
BHOH20
BHOH42
BHOH63

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 791
ChainResidue
AARG444
ALEU468
BHOH70
BHOH125
BHOH142
BARG704

site_idAC7
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL B 3969
ChainResidue
AHOH264
ATHR520
AGLN771
BHOH261
BHOH353
BPRO517
BSER746
BGLY748

site_idAC8
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL B 3970
ChainResidue
BHOH3
BHOH13
BHOH17
BHOH41
BHOH272
BTHR505
BTHR677
BPHE678
BLYS747

site_idAC9
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL B 3972
ChainResidue
BHOH163
BHOH171
BHOH305
BLYS454
BTYR464
BALA660
BLYS661
BTHR663
BLYS689

site_idBC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL B 3974
ChainResidue
BHOH297
BHOH331
BARG671
BASP672
BLYS680
BTRP691

site_idBC2
Number of Residues19
DetailsBINDING SITE FOR RESIDUE 9DX B 2
ChainResidue
BTHR503
BARG508
BVAL670
BGLY673
BSER674
BTHR675
BSER706
BMET722
BGLU723
BSER726
BTYR749
BHOH6
BHOH14
BHOH69
BHOH379
BGLU426
BTYR474
BPRO501
BLEU502

site_idBC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 B 5
ChainResidue
BARG417
BTYR759
BASN787

site_idBC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 B 791
ChainResidue
BHOH327
BARG444
BVAL466
BLYS467
BLEU468

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues12
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"21893069","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2ZNS","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3FUZ","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine; by PKC","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

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

site_idSWS_FT_FI4
Number of Residues4
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

246704

PDB entries from 2025-12-24

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