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1X0I

Crystal Structure of the Acid Blue Form of Bacteriorhodopsin

Functional Information from GO Data
ChainGOidnamespacecontents
10005216molecular_functionmonoatomic ion channel activity
10005886cellular_componentplasma membrane
10006811biological_processmonoatomic ion transport
10007602biological_processphototransduction
10009881molecular_functionphotoreceptor activity
10015454molecular_functionlight-driven active monoatomic ion transmembrane transporter activity
10016020cellular_componentmembrane
11902600biological_processproton transmembrane transport
Functional Information from PDB Data
site_idAC1
Number of Residues10
DetailsBINDING SITE FOR RESIDUE SO4 1 700
ChainResidue
1PRO77
1HOH612
1ARG82
1SER193
1GLU194
1LEU201
1GLU204
1HOH607
1HOH608
1HOH609

site_idAC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE RET 1 250
ChainResidue
1TRP86
1TRP138
1SER141
1THR142
1TRP182
1TYR185
1PRO186
1ASP212
1LYS216

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE L3P 1 260
ChainResidue
1LEU25
1LYS40
1ALA44
1PHE54
1THR107
1ILE117
1TYR147
1HOH635

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE L2P 1 270
ChainResidue
1THR55
1MET56
1PHE88
1THR121
1LEU123
1VAL124
1LEU127

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE L3P 1 280
ChainResidue
1VAL136
1ALA139
1ILE140

site_idAC6
Number of Residues1
DetailsBINDING SITE FOR RESIDUE L3P 1 290
ChainResidue
1LEU15

Functional Information from PROSITE/UniProt
site_idPS00327
Number of Residues12
DetailsBACTERIAL_OPSIN_RET Bacterial rhodopsins retinal binding site. FMVLDVsAKvGF
ChainResidueDetails
1PHE208-PHE219

site_idPS00950
Number of Residues13
DetailsBACTERIAL_OPSIN_1 Bacterial rhodopsins signature 1. RYaDWlFTTPLLL
ChainResidueDetails
1ARG82-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
1GLN1-GLU9
1GLY63-TYR79
1THR128-ARG134
1GLY192-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
1TRP10-VAL29

site_idSWS_FT_FI3
Number of Residues40
DetailsTOPO_DOM: Cytoplasmic => ECO:0000269|PubMed:10452895, ECO:0000269|PubMed:28008064, ECO:0007744|PDB:1C3W
ChainResidueDetails
1LYS30-TYR43
1LEU97-THR107
1GLY155-LYS172

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
1ALA44-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
1TRP80-ASP96

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
1ILE108-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
1PHE135-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
1VAL173-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
1GLU204-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
1ASP85

site_idSWS_FT_FI11
Number of Residues1
DetailsMOD_RES: Pyrrolidone carboxylic acid => ECO:0000269|PubMed:9541408
ChainResidueDetails
1GLN1

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
1LYS216

222624

PDB entries from 2024-07-17

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