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1C8S

BACTERIORHODOPSIN D96N LATE M STATE INTERMEDIATE

Functional Information from GO Data
ChainGOidnamespacecontents
A0005216molecular_functionmonoatomic ion channel activity
A0006811biological_processmonoatomic ion transport
A0016020cellular_componentmembrane
Functional Information from PDB Data
site_idAC1
Number of Residues11
DetailsBINDING SITE FOR RESIDUE LI1 A 601
ChainResidue
AILE11
ALI1612
ASQU701
APHE54
ALEU58
ALEU62
AVAL136
AILE140
AALA143
ALI1606
ALI1608

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE LI1 A 602
ChainResidue
ATRP12
ATYR131
APHE135
ATRP138
AALA139
AALA196
ALI1603
ALI1608

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE LI1 A 603
ChainResidue
ALEU190
AALA196
AVAL199
APRO200
ALI1602
ALI1610

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE LI1 A 605
ChainResidue
AALA18
ALEU22
ALI1606

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE LI1 A 606
ChainResidue
ATHR17
AALA18
ALEU22
ALI1601
ALI1605

site_idAC6
Number of Residues10
DetailsBINDING SITE FOR RESIDUE LI1 A 607
ChainResidue
AILE52
AMET56
ATYR64
ATRP80
ATRP80
ALEU87
AGLY116
AILE117
AVAL124
ALEU127

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE LI1 A 608
ChainResidue
AILE222
ALI1601
ALI1602
ASQU701

site_idAC8
Number of Residues2
DetailsBINDING SITE FOR RESIDUE LI1 A 609
ChainResidue
AVAL177
ALI1610

site_idAC9
Number of Residues8
DetailsBINDING SITE FOR RESIDUE LI1 A 610
ChainResidue
AASN176
AVAL179
AVAL180
ASER183
AALA184
AVAL187
ALI1603
ALI1609

site_idBC1
Number of Residues13
DetailsBINDING SITE FOR RESIDUE LI1 A 612
ChainResidue
AGLY21
ATHR24
ALEU28
AALA44
ATHR47
ALEU48
AALA51
APHE54
AALA110
AILE117
AALA144
ATYR147
ALI1601

site_idBC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE LI1 A 613
ChainResidue
ALEU87
ALEU95

site_idBC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SQU A 701
ChainResidue
ALEU25
ATYR26
ASER214
ALEU221
ALI1601
ALI1608

site_idBC4
Number of Residues11
DetailsBINDING SITE FOR RESIDUE RET A 301
ChainResidue
ATRP86
ATHR90
ALEU93
AGLY122
ATRP138
ASER141
ATRP182
ATYR185
AASP212
AALA215
ALYS216

Functional Information from PROSITE/UniProt
site_idPS00327
Number of Residues12
DetailsBACTERIAL_OPSIN_RET Bacterial rhodopsins retinal binding site. FMVLDVsAKvGF
ChainResidueDetails
APHE208-PHE219

site_idPS00950
Number of Residues13
DetailsBACTERIAL_OPSIN_1 Bacterial rhodopsins signature 1. RYaDWlFTTPLLL
ChainResidueDetails
AARG82-LEU94

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues41
DetailsTOPO_DOM: Extracellular => ECO:0000269|PubMed:10452895, ECO:0000269|PubMed:28008064, ECO:0007744|PDB:1C3W
ChainResidueDetails
AALA14-LEU22
AASN76-LEU92
ASER141-TYR147

site_idSWS_FT_FI2
Number of Residues19
DetailsTRANSMEM: Helical; Name=Helix A => ECO:0000269|PubMed:10452895, ECO:0000269|PubMed:28008064, ECO:0007744|PDB:1C3W
ChainResidueDetails
AGLY23-PHE42

site_idSWS_FT_FI3
Number of Residues40
DetailsTOPO_DOM: Cytoplasmic => ECO:0000269|PubMed:10452895, ECO:0000269|PubMed:28008064, ECO:0007744|PDB:1C3W
ChainResidueDetails
ATYR43-MET56
AALA110-GLY120
ALEU190-LEU207

site_idSWS_FT_FI4
Number of Residues18
DetailsTRANSMEM: Helical; Name=Helix B => ECO:0000269|PubMed:10452895, ECO:0000269|PubMed:28008064, ECO:0007744|PDB:1C3W
ChainResidueDetails
ATYR57-GLN75

site_idSWS_FT_FI5
Number of Residues16
DetailsTRANSMEM: Helical; Name=Helix C => ECO:0000269|PubMed:10452895, ECO:0000269|PubMed:28008064, ECO:0007744|PDB:1C3W
ChainResidueDetails
ALEU93-LEU109

site_idSWS_FT_FI6
Number of Residues19
DetailsTRANSMEM: Helical; Name=Helix D => ECO:0000269|PubMed:10452895, ECO:0000269|PubMed:28008064, ECO:0007744|PDB:1C3W
ChainResidueDetails
ATHR121-ILE140

site_idSWS_FT_FI7
Number of Residues19
DetailsTRANSMEM: Helical; Name=Helix E => ECO:0000269|PubMed:10452895, ECO:0000269|PubMed:28008064, ECO:0007744|PDB:1C3W
ChainResidueDetails
AILE148-TRP189

site_idSWS_FT_FI8
Number of Residues18
DetailsTRANSMEM: Helical; Name=Helix F => ECO:0000269|PubMed:10452895, ECO:0000269|PubMed:28008064, ECO:0007744|PDB:1C3W
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues1
DetailsSITE: Primary proton acceptor => ECO:0000305|PubMed:10903866, ECO:0000305|PubMed:10949309, ECO:0000305|PubMed:28008064
ChainResidueDetails
AALA98

site_idSWS_FT_FI10
Number of Residues1
DetailsMOD_RES: Pyrrolidone carboxylic acid => ECO:0000269|PubMed:9541408
ChainResidueDetails
AALA14

218853

PDB entries from 2024-04-24

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