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3EAM

An open-pore structure of a bacterial pentameric ligand-gated ion channel

Functional Information from GO Data
ChainGOidnamespacecontents
A0004888molecular_functiontransmembrane signaling receptor activity
A0005216molecular_functionmonoatomic ion channel activity
A0005230molecular_functionextracellular ligand-gated monoatomic ion channel activity
A0006811biological_processmonoatomic ion transport
A0016020cellular_componentmembrane
A0034220biological_processmonoatomic ion transmembrane transport
B0004888molecular_functiontransmembrane signaling receptor activity
B0005216molecular_functionmonoatomic ion channel activity
B0005230molecular_functionextracellular ligand-gated monoatomic ion channel activity
B0006811biological_processmonoatomic ion transport
B0016020cellular_componentmembrane
B0034220biological_processmonoatomic ion transmembrane transport
C0004888molecular_functiontransmembrane signaling receptor activity
C0005216molecular_functionmonoatomic ion channel activity
C0005230molecular_functionextracellular ligand-gated monoatomic ion channel activity
C0006811biological_processmonoatomic ion transport
C0016020cellular_componentmembrane
C0034220biological_processmonoatomic ion transmembrane transport
D0004888molecular_functiontransmembrane signaling receptor activity
D0005216molecular_functionmonoatomic ion channel activity
D0005230molecular_functionextracellular ligand-gated monoatomic ion channel activity
D0006811biological_processmonoatomic ion transport
D0016020cellular_componentmembrane
D0034220biological_processmonoatomic ion transmembrane transport
E0004888molecular_functiontransmembrane signaling receptor activity
E0005216molecular_functionmonoatomic ion channel activity
E0005230molecular_functionextracellular ligand-gated monoatomic ion channel activity
E0006811biological_processmonoatomic ion transport
E0016020cellular_componentmembrane
E0034220biological_processmonoatomic ion transmembrane transport
Functional Information from PDB Data
site_idAC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE LMT A 501
ChainResidue
AILE240
ATHR244
AASN245
BLYS33
BTHR244
BLMT501
EALA237
ELMT602

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PC1 A 602
ChainResidue
ATYR194
ALEU203
ATYR254
AASN307
APHE121

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PC1 A 603
ChainResidue
APHE265
AARG287
AILE291
AALA294
APHE299
APC1601

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PC1 A 601
ChainResidue
AVAL275
ATYR278
AGLU282
APC1603
ETRP217

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PC1 B 601
ChainResidue
ATRP217
ALEU304
BTYR278
BGLU282
BARG287
BPC1603

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE LMT B 501
ChainResidue
AALA237
ALMT501
BILE240
BTHR244
BASN245
CLYS33

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PC1 B 602
ChainResidue
BTYR194
BILE198
BTYR254
BASN307
BPHE315

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PC1 B 603
ChainResidue
BILE291
BALA294
BPHE299
BPC1601

site_idAC9
Number of Residues6
DetailsBINDING SITE FOR RESIDUE LMT C 502
ChainResidue
ASER230
CSER230
CILE233
CLMT501
ESER230
ELMT602

site_idBC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PC1 C 601
ChainResidue
BTRP217
CTYR278
CLEU279
CGLU282
CGLN284

site_idBC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE LMT C 501
ChainResidue
BALA237
CILE240
CTHR244
CASN245
CLMT502
DLYS33
ELMT501

site_idBC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE PC1 C 602
ChainResidue
CSER191
CTYR194
CILE198
CLEU203
CLEU206
CTYR254
CASN307
CPHE315

site_idBC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PC1 C 603
ChainResidue
CPHE265
CARG287
CALA294
CPHE299

site_idBC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PC1 D 601
ChainResidue
CTRP217
DTYR278
DGLU282
DARG287
DPC1603

site_idBC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PC1 D 602
ChainResidue
DTYR194
DTYR254
DASN307
DPHE315

site_idBC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PC1 D 603
ChainResidue
DARG287
DALA294
DPHE299
DPC1601

site_idBC8
Number of Residues9
DetailsBINDING SITE FOR RESIDUE LMT E 501
ChainResidue
CLMT501
DALA237
DILE240
DLEU241
DTHR244
DASN245
ELYS33
ETHR244
ELMT602

site_idBC9
Number of Residues8
DetailsBINDING SITE FOR RESIDUE LMT E 602
ChainResidue
CLMT502
EASP31
EILE240
ETHR244
EASN245
ELMT501
ALYS33
ALMT501

site_idCC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE PC1 E 601
ChainResidue
DPHE210
DTRP217
ETYR278
EGLU282
EGLN284
EARG287
EPC1604

site_idCC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PC1 E 603
ChainResidue
EARG118
ESER191
ETYR194
ETYR254
EILE258
EASN307

site_idCC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PC1 E 604
ChainResidue
EARG287
EALA294
EALA298
EPHE299
EPC1601

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues990
DetailsTOPO_DOM: Periplasmic => ECO:0000255
ChainResidueDetails
AGLN2-GLN193
EASN245-MET252
AASN245-MET252
BGLN2-GLN193
BASN245-MET252
CGLN2-GLN193
CASN245-MET252
DGLN2-GLN193
DASN245-MET252
EGLN2-GLN193

site_idSWS_FT_FI2
Number of Residues530
DetailsTRANSMEM: Helical
ChainResidueDetails
ATYR194-PHE216
CSER220-THR244
CTHR253-VAL281
CPRO285-PHE317
DTYR194-PHE216
DSER220-THR244
DTHR253-VAL281
DPRO285-PHE317
ETYR194-PHE216
ESER220-THR244
ETHR253-VAL281
ASER220-THR244
EPRO285-PHE317
ATHR253-VAL281
APRO285-PHE317
BTYR194-PHE216
BSER220-THR244
BTHR253-VAL281
BPRO285-PHE317
CTYR194-PHE216

site_idSWS_FT_FI3
Number of Residues20
DetailsTOPO_DOM: Cytoplasmic => ECO:0000255
ChainResidueDetails
ATRP217-THR219
EGLU282-GLN284
AGLU282-GLN284
BTRP217-THR219
BGLU282-GLN284
CTRP217-THR219
CGLU282-GLN284
DTRP217-THR219
DGLU282-GLN284
ETRP217-THR219

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PDB entries from 2024-07-10

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