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Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1QHJ

X-RAY STRUCTURE OF BACTERIORHODOPSIN GROWN IN LIPIDIC CUBIC PHASES

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 RET A 300

Chain	Residue
A	PRO186
A	TRP189
A	ASP212
A	ALA215
A	LYS216
A	TRP86
A	THR90
A	MET118
A	TRP138
A	SER141
A	THR142
A	TRP182
A	TYR185

site_id	AC2
Number of Residues	13
Details	BINDING SITE FOR RESIDUE PH1 A 500

Chain	Residue
A	LEU48
A	ILE52
A	MET56
A	TYR64
A	TRP80
A	LEU87
A	PHE88
A	LEU92
A	GLY116
A	ILE117
A	LEU123
A	VAL124
A	LEU127

site_id	AC3
Number of Residues	14
Details	BINDING SITE FOR RESIDUE PH1 A 501

Chain	Residue
A	ALA14
A	THR17
A	ALA18
A	GLY21
A	THR24
A	LEU25
A	PHE54
A	LEU58
A	TYR133
A	ALA139
A	ILE140
A	PH1504
A	PH1504
A	PH1506

site_id	AC4
Number of Residues	14
Details	BINDING SITE FOR RESIDUE PH1 A 502

Chain	Residue
A	TRP12
A	LEU15
A	TYR131
A	PHE135
A	TRP138
A	ALA139
A	ALA196
A	PRO200
A	ASN202
A	ILE203
A	LEU206
A	MET209
A	VAL210
A	PH1503

site_id	AC5
Number of Residues	13
Details	BINDING SITE FOR RESIDUE PH1 A 503

Chain	Residue
A	VAL187
A	ILE191
A	ALA196
A	ILE198
A	ILE198
A	VAL199
A	PRO200
A	LEU207
A	VAL210
A	LEU211
A	PH1502
A	PH1505
A	PH1508

site_id	AC6
Number of Residues	9
Details	BINDING SITE FOR RESIDUE PH1 A 504

Chain	Residue
A	TRP10
A	ILE11
A	ALA14
A	LEU15
A	LEU22
A	LEU22
A	PH1501
A	PH1501
A	PH1508

site_id	AC7
Number of Residues	10
Details	BINDING SITE FOR RESIDUE PH1 A 505

Chain	Residue
A	LYS172
A	ARG175
A	ASN176
A	VAL179
A	VAL180
A	SER183
A	VAL187
A	PH1503
A	PH1507
A	PH1507

site_id	AC8
Number of Residues	14
Details	BINDING SITE FOR RESIDUE PH1 A 506

Chain	Residue
A	TYR150
A	PH1501
A	LEU28
A	LYS40
A	TYR43
A	ALA44
A	THR47
A	LEU48
A	THR107
A	ALA110
A	ILE117
A	ILE140
A	ALA144
A	TYR147

site_id	AC9
Number of Residues	15
Details	BINDING SITE FOR RESIDUE PH1 A 507

Chain	Residue
A	MET145
A	LEU146
A	LEU149
A	TYR150
A	PHE153
A	PHE154
A	LYS172
A	VAL173
A	ASN176
A	VAL177
A	VAL180
A	SER183
A	PH1505
A	PH1505
A	PH1508

site_id	BC1
Number of Residues	14
Details	BINDING SITE FOR RESIDUE PH1 A 508

Chain	Residue
A	LEU19
A	TYR26
A	MET32
A	LEU146
A	VAL210
A	VAL213
A	SER214
A	VAL217
A	GLY218
A	LEU221
A	ARG225
A	PH1503
A	PH1504
A	PH1507

site_id	SFF
Number of Residues	1
Details	SCHIFF BASE

Chain	Residue
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	GLN1-GLU9
A	GLY63-TYR79
A	THR128-ARG134
A	GLY192-ILE203

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	TRP10-VAL29

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	LYS30-TYR43
A	LEU97-THR107
A	GLY155-LYS172

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	ALA44-LEU62

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	TRP80-ASP96

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	ILE108-LEU127

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	PHE135-PHE154

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	VAL173-ILE191

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	GLU204-LEU223

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	ASP85

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

Chain	Residue	Details
A	GLN1

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	LYS216

219140

PDB entries from 2024-05-01

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