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5BUU

Crystal structure of the GluA2 ligand-binding domain (L483Y-N754S) in complex with glutamate and BPAM-321 at 2.07 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 Residues10
Detailsbinding site for residue 4V6 A 801
ChainResidue
AILE481
B4V6801
ASER497
ALYS730
AGLY731
ASO4805
BLYS493
BPRO494
BSER497
BSER754

site_idAC2
Number of Residues11
Detailsbinding site for residue GLU A 802
ChainResidue
ATYR450
APRO478
ALEU479
ATHR480
AARG485
AGLY653
ASER654
ATHR655
AGLU705
AHOH923
AHOH938

site_idAC3
Number of Residues7
Detailsbinding site for residue SO4 A 803
ChainResidue
ASER652
ALYS656
AARG660
AHOH905
AHOH909
AHOH911
AHOH961

site_idAC4
Number of Residues6
Detailsbinding site for residue SO4 A 804
ChainResidue
APRO494
ALEU751
AHOH903
BLYS730
BGLY731
B4V6801

site_idAC5
Number of Residues5
Detailsbinding site for residue SO4 A 805
ChainResidue
ALYS730
AGLY731
A4V6801
BLYS493
BPRO494

site_idAC6
Number of Residues12
Detailsbinding site for residue 4V6 B 801
ChainResidue
ALYS493
APRO494
ASER497
ALEU751
ASER754
A4V6801
ASO4804
AHOH903
BILE481
BSER497
BLYS730
BGLY731

site_idAC7
Number of Residues12
Detailsbinding site for residue GLU B 802
ChainResidue
BTYR450
BPRO478
BLEU479
BTHR480
BARG485
BGLY653
BSER654
BTHR655
BGLU705
BHOH911
BHOH919
BHOH922

site_idAC8
Number of Residues6
Detailsbinding site for residue SO4 B 803
ChainResidue
BALA452
BSER652
BLYS656
BARG660
BHOH902
BHOH908

site_idAC9
Number of Residues3
Detailsbinding site for residue SO4 B 804
ChainResidue
ALYS695
BARG420
BHOH907

site_idAD1
Number of Residues5
Detailsbinding site for residue EDO B 805
ChainResidue
ATYR483
BHIS435
BALA745
BLEU748
BALA749

site_idAD2
Number of Residues3
Detailsbinding site for residue EDO B 806
ChainResidue
AASN726
ASER729
BASP760

site_idAD3
Number of Residues5
Detailsbinding site for residue EDO B 807
ChainResidue
ALYS493
BGLU486
BASP490
BPHE491
BHOH913

site_idAD4
Number of Residues3
Detailsbinding site for residue EDO B 808
ChainResidue
AASP760
BASP728
BSER729

site_idAD5
Number of Residues3
Detailsbinding site for residue EDO B 809
ChainResidue
BARG660
BTRP671
BARG675

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues12
DetailsBINDING: BINDING => ECO:0000269|PubMed:11086992, ECO:0000269|PubMed:16483599, ECO:0007744|PDB:1FTJ, ECO:0007744|PDB:2CMO
ChainResidueDetails
APRO478
BSER654
BTHR655
BGLU705
ATHR480
AARG485
ASER654
ATHR655
AGLU705
BPRO478
BTHR480
BARG485

site_idSWS_FT_FI2
Number of Residues6
DetailsSITE: Interaction with the cone snail toxin Con-ikot-ikot => ECO:0000269|PubMed:25103405
ChainResidueDetails
AARG453
AARG660
ALYS752
BARG453
BARG660
BLYS752

site_idSWS_FT_FI3
Number of Residues2
DetailsSITE: Crucial to convey clamshell closure to channel opening => ECO:0000269|PubMed:25103405
ChainResidueDetails
AILE633
BILE633

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphoserine; by PKC => ECO:0000269|PubMed:8848293
ChainResidueDetails
ASER662
BSER662

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphoserine; by PKG => ECO:0000269|PubMed:8848293
ChainResidueDetails
ASER696
BSER696

site_idSWS_FT_FI6
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN392
BASN392

222624

PDB entries from 2024-07-17

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