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Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2BRD

CRYSTAL STRUCTURE OF BACTERIORHODOPSIN IN PURPLE MEMBRANE

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005216	molecular_function	monoatomic ion channel activity
A	0005886	cellular_component	plasma membrane
A	0006811	biological_process	monoatomic ion transport
A	0007602	biological_process	phototransduction
A	0009881	molecular_function	photoreceptor activity
A	0015454	molecular_function	light-driven active monoatomic ion transmembrane transporter activity
A	0016020	cellular_component	membrane
A	1902600	biological_process	proton transmembrane transport

Functional Information from PDB Data

site_id	AC1
Number of Residues	13
Details	BINDING SITE FOR RESIDUE DPG A 261

Chain	Residue
A	TYR64
A	VAL124
A	LYS129
A	DPG266
A	DPG266
A	LEU66
A	LEU66
A	MET68
A	PRO70
A	TRP80
A	LEU87
A	PHE88
A	PHE88

site_id	AC2
Number of Residues	12
Details	BINDING SITE FOR RESIDUE DPG A 262

Chain	Residue
A	SER183
A	VAL187
A	ILE191
A	ILE191
A	ALA196
A	ILE198
A	ILE198
A	LEU207
A	DPG263
A	DPG267
A	DPG267
A	DPG268

site_id	AC3
Number of Residues	11
Details	BINDING SITE FOR RESIDUE DPG A 263

Chain	Residue
A	TRP12
A	PHE135
A	TRP138
A	ALA196
A	ILE203
A	LEU206
A	VAL210
A	DPG262
A	DPG264
A	DPG265
A	DPG268

site_id	AC4
Number of Residues	8
Details	BINDING SITE FOR RESIDUE DPG A 264

Chain	Residue
A	ALA18
A	PHE54
A	LEU58
A	LEU61
A	VAL136
A	DPG263
A	DPG265
A	DPG270

site_id	AC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE DPG A 265

Chain	Residue
A	ILE11
A	LEU15
A	ALA18
A	DPG263
A	DPG264

site_id	AC6
Number of Residues	15
Details	BINDING SITE FOR RESIDUE DPG A 266

Chain	Residue
A	ILE52
A	PHE88
A	PHE88
A	LEU92
A	LEU95
A	LEU99
A	ALA103
A	GLN105
A	GLN105
A	ILE108
A	LEU109
A	GLY116
A	ILE117
A	DPG261
A	DPG261

site_id	AC7
Number of Residues	10
Details	BINDING SITE FOR RESIDUE DPG A 267

Chain	Residue
A	PHE156
A	LYS172
A	ARG175
A	ASN176
A	VAL180
A	ALA184
A	VAL187
A	DPG262
A	DPG262
A	DPG268

site_id	AC8
Number of Residues	18
Details	BINDING SITE FOR RESIDUE DPG A 268

Chain	Residue
A	TRP138
A	THR142
A	MET145
A	LEU149
A	TYR150
A	PHE153
A	THR157
A	SER169
A	LYS172
A	VAL173
A	VAL179
A	PRO186
A	VAL210
A	SER214
A	ARG225
A	DPG262
A	DPG263
A	DPG267

site_id	AC9
Number of Residues	10
Details	BINDING SITE FOR RESIDUE DPG A 269

Chain	Residue
A	PHE154
A	LEU221
A	DPG270
A	LEU28
A	MET32
A	GLY33
A	LYS40
A	THR47
A	ALA51
A	TYR147

site_id	BC1
Number of Residues	10
Details	BINDING SITE FOR RESIDUE DPG A 270

Chain	Residue
A	LEU22
A	TYR26
A	VAL29
A	VAL29
A	LYS30
A	GLY33
A	LEU224
A	ARG227
A	DPG264
A	DPG269

site_id	BC2
Number of Residues	11
Details	BINDING SITE FOR RESIDUE RET A 271

Chain	Residue
A	TRP86
A	THR89
A	THR90
A	MET118
A	TRP138
A	SER141
A	TRP182
A	TYR185
A	TRP189
A	ASP212
A	LYS216

Functional Information from PROSITE/UniProt

site_id	PS00327
Number of Residues	12
Details	BACTERIAL_OPSIN_RET Bacterial rhodopsins retinal binding site. FMVLDVsAKvGF

Chain	Residue	Details
A	PHE208-PHE219

site_id	PS00950
Number of Residues	13
Details	BACTERIAL_OPSIN_1 Bacterial rhodopsins signature 1. RYaDWlFTTPLLL

Chain	Residue	Details
A	ARG82-LEU94

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	41
Details	TOPO_DOM: Extracellular => ECO:0000269\|PubMed:10452895, ECO:0000269\|PubMed:28008064, ECO:0007744\|PDB:1C3W

Chain	Residue	Details
A	ALA2-TRP10
A	TYR64-TRP80
A	LYS129-PHE135
A	SER193-GLU204

site_id	SWS_FT_FI2
Number of Residues	19
Details	TRANSMEM: Helical; Name=Helix A => ECO:0000269\|PubMed:10452895, ECO:0000269\|PubMed:28008064, ECO:0007744\|PDB:1C3W

Chain	Residue	Details
A	ILE11-LYS30

site_id	SWS_FT_FI3
Number of Residues	40
Details	TOPO_DOM: Cytoplasmic => ECO:0000269\|PubMed:10452895, ECO:0000269\|PubMed:28008064, ECO:0007744\|PDB:1C3W

Chain	Residue	Details
A	GLY31-ALA44
A	ALA98-ILE108
A	PHE156-VAL173

site_id	SWS_FT_FI4
Number of Residues	18
Details	TRANSMEM: Helical; Name=Helix B => ECO:0000269\|PubMed:10452895, ECO:0000269\|PubMed:28008064, ECO:0007744\|PDB:1C3W

Chain	Residue	Details
A	ILE45-GLY63

site_id	SWS_FT_FI5
Number of Residues	16
Details	TRANSMEM: Helical; Name=Helix C => ECO:0000269\|PubMed:10452895, ECO:0000269\|PubMed:28008064, ECO:0007744\|PDB:1C3W

Chain	Residue	Details
A	ALA81-LEU97

site_id	SWS_FT_FI6
Number of Residues	19
Details	TRANSMEM: Helical; Name=Helix D => ECO:0000269\|PubMed:10452895, ECO:0000269\|PubMed:28008064, ECO:0007744\|PDB:1C3W

Chain	Residue	Details
A	LEU109-THR128

site_id	SWS_FT_FI7
Number of Residues	19
Details	TRANSMEM: Helical; Name=Helix E => ECO:0000269\|PubMed:10452895, ECO:0000269\|PubMed:28008064, ECO:0007744\|PDB:1C3W

Chain	Residue	Details
A	VAL136-GLY155

site_id	SWS_FT_FI8
Number of Residues	18
Details	TRANSMEM: Helical; Name=Helix F => ECO:0000269\|PubMed:10452895, ECO:0000269\|PubMed:28008064, ECO:0007744\|PDB:1C3W

Chain	Residue	Details
A	LEU174-GLY192

site_id	SWS_FT_FI9
Number of Residues	19
Details	TRANSMEM: Helical; Name=Helix G => ECO:0000269\|PubMed:10452895, ECO:0000269\|PubMed:28008064, ECO:0007744\|PDB:1C3W

Chain	Residue	Details
A	THR205-LEU224

site_id	SWS_FT_FI10
Number of Residues	1
Details	SITE: Primary proton acceptor => ECO:0000305\|PubMed:10903866, ECO:0000305\|PubMed:10949309, ECO:0000305\|PubMed:28008064

Chain	Residue	Details
A	TRP86

site_id	SWS_FT_FI11
Number of Residues	1
Details	MOD_RES: Pyrrolidone carboxylic acid => ECO:0000269\|PubMed:9541408

Chain	Residue	Details
A	ALA2

site_id	SWS_FT_FI12
Number of Residues	1
Details	MOD_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

Chain	Residue	Details
A	VAL217

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