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5EGI

Structure of a Trimeric Intracellular Cation channel from C. elegans with bound Ca2+

Functional Information from GO Data
ChainGOidnamespacecontents
A0005267molecular_functionpotassium channel activity
A0016020cellular_componentmembrane
A0042802molecular_functionidentical protein binding
A0071805biological_processpotassium ion transmembrane transport
B0005267molecular_functionpotassium channel activity
B0016020cellular_componentmembrane
B0042802molecular_functionidentical protein binding
B0071805biological_processpotassium ion transmembrane transport
C0005267molecular_functionpotassium channel activity
C0016020cellular_componentmembrane
C0042802molecular_functionidentical protein binding
C0071805biological_processpotassium ion transmembrane transport
Functional Information from PDB Data
site_idAC1
Number of Residues17
Detailsbinding site for residue PT5 A 301
ChainResidue
AGLU41
AHIS184
AGLU186
APRO190
ASER191
ATHR194
BSER60
BSER64
BARG177
AMET68
ALYS129
AARG133
AALA164
AGLY165
ASER166
AGLY167
AARG170

site_idAC2
Number of Residues18
Detailsbinding site for residue PT5 B 301
ChainResidue
BGLU41
BLEU79
BLYS129
BARG133
BALA164
BSER166
BGLY167
BILE168
BARG170
BHIS184
BGLU186
BALA193
BTHR194
CLEU63
CLEU67
CPHE74
CARG177
CDMU302

site_idAC3
Number of Residues6
Detailsbinding site for residue CA B 302
ChainResidue
BHOH401
BHOH401
BHOH402
BHOH402
CHOH404
CHOH404

site_idAC4
Number of Residues17
Detailsbinding site for residue PT5 C 301
ChainResidue
ALEU67
ALEU172
CGLU41
CMET68
CPHE78
CLYS129
CARG133
CTHR160
CALA164
CGLY165
CSER166
CGLY167
CILE168
CARG170
CHIS184
CPRO190
CTHR194

site_idAC5
Number of Residues8
Detailsbinding site for residue DMU C 302
ChainResidue
BLEU157
BTHR194
BVAL198
BPT5301
CPHE53
CHIS57
CLEU59
CSER60

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues117
DetailsTOPO_DOM: Lumenal => ECO:0000305|PubMed:27698420
ChainResidueDetails
AMET1-TYR27
CGLY81-LYS89
CPRO149-ASN150
CTHR211-ALA215
AGLY81-LYS89
APRO149-ASN150
ATHR211-ALA215
BMET1-TYR27
BGLY81-LYS89
BPRO149-ASN150
BTHR211-ALA215
CMET1-TYR27

site_idSWS_FT_FI2
Number of Residues51
DetailsTRANSMEM: Helical;Name=1 => ECO:0000269|PubMed:27698420
ChainResidueDetails
APRO28-ASP45
BPRO28-ASP45
CPRO28-ASP45

site_idSWS_FT_FI3
Number of Residues93
DetailsTOPO_DOM: Cytoplasmic => ECO:0000305|PubMed:27698420
ChainResidueDetails
ALEU46-LYS56
APRO108-THR119
AGLY178-LEU188
BLEU46-LYS56
BPRO108-THR119
BGLY178-LEU188
CLEU46-LYS56
CPRO108-THR119
CGLY178-LEU188

site_idSWS_FT_FI4
Number of Residues69
DetailsTRANSMEM: Discontinuously helical;Name=2 => ECO:0000269|PubMed:27698420
ChainResidueDetails
AHIS57-LEU80
BHIS57-LEU80
CHIS57-LEU80

site_idSWS_FT_FI5
Number of Residues51
DetailsTRANSMEM: Helical;Name=3 => ECO:0000269|PubMed:27698420
ChainResidueDetails
AARG90-ALA107
BARG90-ALA107
CARG90-ALA107

site_idSWS_FT_FI6
Number of Residues84
DetailsTRANSMEM: Helical;Name=4 => ECO:0000269|PubMed:27698420
ChainResidueDetails
APRO120-TYR148
BPRO120-TYR148
CPRO120-TYR148

site_idSWS_FT_FI7
Number of Residues78
DetailsTRANSMEM: Discontinuously helical;Name=5 => ECO:0000269|PubMed:27698420
ChainResidueDetails
ASER151-ARG177
BSER151-ARG177
CSER151-ARG177

site_idSWS_FT_FI8
Number of Residues63
DetailsTRANSMEM: Helical;Name=6 => ECO:0000269|PubMed:27698420
ChainResidueDetails
AARG189-GLY210
BARG189-GLY210
CARG189-GLY210

site_idSWS_FT_FI9
Number of Residues69
DetailsTRANSMEM: Helical;Name=7 => ECO:0000269|PubMed:27698420
ChainResidueDetails
APRO216-HIS239
BPRO216-HIS239
CPRO216-HIS239

site_idSWS_FT_FI10
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:27698420, ECO:0007744|PDB:5EGI
ChainResidueDetails
ALYS129
AARG133
BLYS129
BARG133
CLYS129
CARG133

site_idSWS_FT_FI11
Number of Residues3
DetailsBINDING: BINDING => ECO:0007744|PDB:5EGI
ChainResidueDetails
ASER166
BSER166
CSER166

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PDB entries from 2024-07-17

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