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1KG9

Structure of a "mock-trapped" early-M intermediate of bacteriorhosopsin

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 Residues12
DetailsBINDING SITE FOR RESIDUE RET A 301
ChainResidue
ATRP86
ATRP189
AASP212
ALYS216
ATHR89
ATHR90
AMET118
ATRP138
ASER141
ATHR142
ATRP182
ATYR185

site_idAC2
Number of Residues1
DetailsBINDING SITE FOR RESIDUE LI1 A 602
ChainResidue
AILE203

site_idAC3
Number of Residues1
DetailsBINDING SITE FOR RESIDUE LI1 A 605
ChainResidue
AILE198

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE LI1 A 606
ChainResidue
AALA18
ALEU22
ALEU61

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE LI1 A 607
ChainResidue
AMET56
APHE88
AGLY116
AILE117

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE LI1 A 609
ChainResidue
APHE154
AVAL173
AVAL177
ALI1610

site_idAC7
Number of Residues2
DetailsBINDING SITE FOR RESIDUE LI1 A 610
ChainResidue
AASN176
ALI1609

site_idAC8
Number of Residues9
DetailsBINDING SITE FOR RESIDUE LI1 A 612
ChainResidue
AGLY21
ATHR24
ALEU28
AALA44
ATHR47
APHE54
AALA110
ATYR147
AHOH512

site_idAC9
Number of Residues3
DetailsBINDING SITE FOR RESIDUE LI1 A 613
ChainResidue
ALEU87
ALEU95
AVAL112

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
AALA2-TRP10
ATYR64-TRP80
ALYS129-PHE135
ASER193-GLU204

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
AILE11-LYS30

site_idSWS_FT_FI3
Number of Residues40
DetailsTOPO_DOM: Cytoplasmic => ECO:0000269|PubMed:10452895, ECO:0000269|PubMed:28008064, ECO:0007744|PDB:1C3W
ChainResidueDetails
AGLY31-ALA44
AALA98-ILE108
APHE156-VAL173

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
AILE45-GLY63

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
AALA81-LEU97

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
ALEU109-THR128

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
AVAL136-GLY155

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
ALEU174-GLY192

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
ATHR205-LEU224

site_idSWS_FT_FI10
Number of Residues1
DetailsSITE: Primary proton acceptor => ECO:0000305|PubMed:10903866, ECO:0000305|PubMed:10949309, ECO:0000305|PubMed:28008064
ChainResidueDetails
ATRP86

site_idSWS_FT_FI11
Number of Residues1
DetailsMOD_RES: Pyrrolidone carboxylic acid => ECO:0000269|PubMed:9541408
ChainResidueDetails
AALA2

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
AVAL217

218853

PDB entries from 2024-04-24

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