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7Z2R

Differences between the GluD1 and GluD2 receptors revealed by GluD1 X-ray crystallography, binding studies and molecular dynamics

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 Residues5
Detailsbinding site for residue SO4 A 301
ChainResidue
ALYS100
AARG101
ASER178
AARG182
AHOH405

site_idAC2
Number of Residues4
Detailsbinding site for residue SO4 A 302
ChainResidue
AARG57
ATYR58
AGLY59
AHIS60

site_idAC3
Number of Residues6
Detailsbinding site for residue SO4 A 303
ChainResidue
ATYR142
ALYS146
ALYS186
ASER218
ASER219
AHOH416

site_idAC4
Number of Residues6
Detailsbinding site for residue SO4 B 301
ChainResidue
BARG57
BTYR58
BGLY59
BHIS60
BASN68
BHOH414

site_idAC5
Number of Residues6
Detailsbinding site for residue SO4 B 302
ChainResidue
BILE88
BLYS100
BARG101
BSER178
BARG182
BHOH407

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues12
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:Q9ULK0
ChainResidueDetails
AGLU93
BASP205
BASP207
BSER209
AVAL96
AASP97
AASP205
AASP207
ASER209
BGLU93
BVAL96
BASP97

site_idSWS_FT_FI2
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000250|UniProtKB:Q9ULK0
ChainResidueDetails
AASN64
BASN64

site_idSWS_FT_FI3
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN176
BASN176

237423

PDB entries from 2025-06-11

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