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2I20

Bacteriorhodopsin/lipid complex, M state of D96A mutant

Functional Information from GO Data
ChainGOidnamespacecontents
A0005216molecular_functionmonoatomic ion channel activity
A0005886cellular_componentplasma membrane
A0006811biological_processmonoatomic ion transport
A0007602biological_processphototransduction
A0009881molecular_functionphotoreceptor activity
A0015454molecular_functionlight-driven active monoatomic ion transmembrane transporter activity
A0016020cellular_componentmembrane
A1902600biological_processproton transmembrane transport
Functional Information from PDB Data
site_idAC1
Number of Residues10
DetailsBINDING SITE FOR RESIDUE RET A 300
ChainResidue
ATRP86
ALYS216
ATHR90
ALEU93
AMET118
ASER141
ATHR142
ATRP182
ATYR185
AASP212

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE LI1 A 601
ChainResidue
AILE11
ALEU58
ATYR133
AVAL136
AILE140
ALI1608
ALI1612

site_idAC3
Number of Residues14
DetailsBINDING SITE FOR RESIDUE LI1 A 602
ChainResidue
ATRP12
ATYR131
APHE135
AVAL136
AALA139
ASER162
AMET163
AARG164
AALA196
AASN202
AILE203
ALEU206
ALEU207
ALI1603

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE LI1 A 603
ChainResidue
AVAL187
ALEU190
AILE198
APRO200
ALI1602
ALI1604

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE LI1 A 604
ChainResidue
AILE191
AILE198
AILE198
ALI1603

site_idAC6
Number of Residues1
DetailsBINDING SITE FOR RESIDUE LI1 A 605
ChainResidue
ALI1611

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE LI1 A 606
ChainResidue
AALA14
ATHR17
AALA18
ALEU22
ALI1611

site_idAC8
Number of Residues7
DetailsBINDING SITE FOR RESIDUE LI1 A 607
ChainResidue
AMET56
ATYR64
ATRP80
ATRP80
AALA84
AGLY116
AILE117

site_idAC9
Number of Residues3
DetailsBINDING SITE FOR RESIDUE LI1 A 608
ChainResidue
ALEU146
ALI1601
ASQU701

site_idBC1
Number of Residues2
DetailsBINDING SITE FOR RESIDUE LI1 A 609
ChainResidue
AASN176
ALI1610

site_idBC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE LI1 A 610
ChainResidue
APHE153
ALYS172
AARG175
AASN176
AVAL179
AVAL180
ASER183
AVAL187
ALI1609

site_idBC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE LI1 A 611
ChainResidue
ALEU22
ALEU25
AVAL29
ALI1605
ALI1606
ASQU701

site_idBC4
Number of Residues9
DetailsBINDING SITE FOR RESIDUE LI1 A 612
ChainResidue
ATHR24
ALEU28
APHE54
AALA110
AALA144
ATYR147
AHOH512
AHOH513
ALI1601

site_idBC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE LI1 A 613
ChainResidue
ALEU95
AHOH511

site_idBC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SQU A 701
ChainResidue
ATYR26
AVAL29
ASER214
AVAL217
ALEU221
ALI1608
ALI1611

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
AGLN1-GLU9
AGLY63-TYR79
ATHR128-ARG134
AGLY192-ILE203

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
ATRP10-VAL29

site_idSWS_FT_FI3
Number of Residues65
DetailsTOPO_DOM: Cytoplasmic => ECO:0000269|PubMed:10452895, ECO:0000269|PubMed:28008064, ECO:0007744|PDB:1C3W
ChainResidueDetails
ALYS30-TYR43
ALEU97-THR107
AGLY155-LYS172
ALEU224-ASP249

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
AALA44-LEU62

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
ATRP80-ALA96

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
AILE108-LEU127

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
APHE135-PHE154

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
AVAL173-ILE191

site_idSWS_FT_FI9
Number of Residues19
DetailsTRANSMEM: Helical; Name=Helix G => ECO:0000269|PubMed:10452895, ECO:0000269|PubMed:28008064, ECO:0007744|PDB:1C3W
ChainResidueDetails
AGLU204-LEU223

site_idSWS_FT_FI10
Number of Residues1
DetailsSITE: Primary proton acceptor => ECO:0000305|PubMed:10903866, ECO:0000305|PubMed:10949309, ECO:0000305|PubMed:28008064
ChainResidueDetails
AASP85

site_idSWS_FT_FI11
Number of Residues1
DetailsMOD_RES: Pyrrolidone carboxylic acid => ECO:0000269|PubMed:9541408
ChainResidueDetails
AGLN1

site_idSWS_FT_FI12
Number of Residues1
DetailsMOD_RES: N6-(retinylidene)lysine => ECO:0000269|PubMed:10452895, ECO:0000269|PubMed:10467143, ECO:0000269|PubMed:10548112, ECO:0000269|PubMed:10903866, ECO:0000269|PubMed:10949307, ECO:0000269|PubMed:10949309, ECO:0000269|PubMed:11829498, ECO:0000269|PubMed:28008064, ECO:0000269|PubMed:6794028, ECO:0000269|PubMed:9287223, ECO:0000269|PubMed:9632391, ECO:0000269|PubMed:9751724, ECO:0007744|PDB:1C3W, ECO:0007744|PDB:1F50, ECO:0007744|PDB:1IW9, ECO:0007744|PDB:1KG8, ECO:0007744|PDB:1KG9, ECO:0007744|PDB:1M0L, ECO:0007744|PDB:1M0M, ECO:0007744|PDB:1O0A, ECO:0007744|PDB:1P8H, ECO:0007744|PDB:1P8U, ECO:0007744|PDB:1Q5J, ECO:0007744|PDB:1QHJ, ECO:0007744|PDB:1QKP, ECO:0007744|PDB:1QM8, ECO:0007744|PDB:1R2N, ECO:0007744|PDB:1R84, ECO:0007744|PDB:1S8J, ECO:0007744|PDB:1TN0, ECO:0007744|PDB:1TN5, ECO:0007744|PDB:1UCQ, ECO:0007744|PDB:1X0I, ECO:0007744|PDB:1X0K, ECO:0007744|PDB:1X0S, ECO:0007744|PDB:1XJI, ECO:0007744|PDB:2AT9, ECO:0007744|PDB:2BRD, ECO:0007744|PDB:2I1X, ECO:0007744|PDB:2I20, ECO:0007744|PDB:2I21, ECO:0007744|PDB:2NTU, ECO:0007744|PDB:2NTW, ECO:0007744|PDB:2WJK, ECO:0007744|PDB:2WJL, ECO:0007744|PDB:2ZFE, ECO:0007744|PDB:2ZZL, ECO:0007744|PDB:3COD, ECO:0007744|PDB:3HAN, ECO:0007744|PDB:3HAO, ECO:0007744|PDB:3HAP, ECO:0007744|PDB:3HAQ, ECO:0007744|PDB:3HAR, ECO:0007744|PDB:3HAS, ECO:0007744|PDB:3NS0, ECO:0007744|PDB:3NSB, ECO:0007744|PDB:3T45, ECO:0007744|PDB:3UTV, ECO:0007744|PDB:3UTW, ECO:0007744|PDB:3UTX, ECO:0007744|PDB:3VHZ, ECO:0007744|PDB:3VI0, ECO:0007744|PDB:4FPD, ECO:0007744|PDB:4HWL, ECO:0007744|PDB:4MD1, ECO:0007744|PDB:4MD2, ECO:0007744|PDB:4X31, ECO:0007744|PDB:4X32, ECO:0007744|PDB:5A44, ECO:0007744|PDB:5A45, ECO:0007744|PDB:5B34, ECO:0007744|PDB:5B6V, ECO:0007744|PDB:5B6W, ECO:0007744|PDB:5B6X, ECO:0007744|PDB:5B6Y, ECO:0007744|PDB:5B6Z, ECO:0007744|PDB:5BR2, ECO:0007744|PDB:5BR5, ECO:0007744|PDB:5H2H, ECO:0007744|PDB:5H2I, ECO:0007744|PDB:5H2J, ECO:0007744|PDB:5H2K, ECO:0007744|PDB:5H2L, ECO:0007744|PDB:5H2M, ECO:0007744|PDB:5H2N, ECO:0007744|PDB:5H2O, ECO:0007744|PDB:5H2P, ECO:0007744|PDB:5J7A
ChainResidueDetails
ALYS216

227344

PDB entries from 2024-11-13

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