3WQJ

Crystal structure of archaerhodopsin-2 at 1.8 angstrom resolution

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	0016020	cellular_component	membrane
A	1902600	biological_process	proton transmembrane transport

Functional Information from PDB Data

site_id	AC1
Number of Residues	12
Details	BINDING SITE FOR RESIDUE RET A 301

Chain	Residue
A	TRP91
A	TRP194
A	ASP217
A	LYS221
A	THR95
A	MET123
A	TRP143
A	SER146
A	THR147
A	TRP187
A	TYR190
A	PRO191

---

site_id	AC2
Number of Residues	11
Details	BINDING SITE FOR RESIDUE 22B A 302

Chain	Residue
A	PHE29
A	GLY35
A	ARG44
A	ALA48
A	ILE51
A	THR112
A	THR115
A	VAL119
A	PHE145
A	TYR156
A	SER160

---

site_id	AC3
Number of Residues	9
Details	BINDING SITE FOR RESIDUE SO4 A 303

Chain	Residue
A	PHE66
A	GLY67
A	ILE68
A	SER133
A	LYS134
A	THR135
A	ALA138
A	HOH409
A	HOH428

---

site_id	AC4
Number of Residues	9
Details	BINDING SITE FOR RESIDUE L2P A 304

Chain	Residue
A	ALA59
A	ALA63
A	TYR85
A	ALA89
A	LEU92
A	VAL125
A	LEU128
A	SQL308
A	SQL308

---

site_id	AC5
Number of Residues	1
Details	BINDING SITE FOR RESIDUE L3P A 305

Chain	Residue
A	ILE26

---

site_id	AC6
Number of Residues	1
Details	BINDING SITE FOR RESIDUE L4P A 306

Chain	Residue
A	ILE113

---

site_id	AC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE L4P A 307

Chain	Residue
A	GLU45
A	ALA48
A	ILE49
A	ARG110

---

site_id	AC8
Number of Residues	2
Details	BINDING SITE FOR RESIDUE SQL A 308

Chain	Residue
A	L2P304
A	L2P304

---

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	PHE213-PHE224

---

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

Chain	Residue	Details
A	ARG87-LEU99

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	39
Details	TOPO_DOM: Extracellular => ECO:0000250

Chain	Residue	Details
A	GLN1-PRO12
A	PHE66-TYR84
A	SER133-PRO136
A	THR198-GLY205

---

site_id	SWS_FT_FI2
Number of Residues	21
Details	TRANSMEM: Helical; Name=Helix A => ECO:0000250

Chain	Residue	Details
A	GLU13-ARG34

---

site_id	SWS_FT_FI3
Number of Residues	26
Details	TOPO_DOM: Cytoplasmic => ECO:0000250

Chain	Residue	Details
A	GLY35-ALA43
A	LYS107-ASP109
A	ALA166-ARG168
A	GLU239-ASP253

---

site_id	SWS_FT_FI4
Number of Residues	21
Details	TRANSMEM: Helical; Name=Helix B => ECO:0000250

Chain	Residue	Details
A	ARG44-PHE65

---

site_id	SWS_FT_FI5
Number of Residues	21
Details	TRANSMEM: Helical; Name=Helix C => ECO:0000250

Chain	Residue	Details
A	TYR85-ALA106

---

site_id	SWS_FT_FI6
Number of Residues	22
Details	TRANSMEM: Helical; Name=Helix D => ECO:0000250

Chain	Residue	Details
A	ARG110-LEU132

---

site_id	SWS_FT_FI7
Number of Residues	28
Details	TRANSMEM: Helical; Name=Helix E => ECO:0000250

Chain	Residue	Details
A	LEU137-ALA165

---

site_id	SWS_FT_FI8
Number of Residues	28
Details	TRANSMEM: Helical; Name=Helix F => ECO:0000250

Chain	Residue	Details
A	SER169-GLY197

---

site_id	SWS_FT_FI9
Number of Residues	32
Details	TRANSMEM: Helical; Name=Helix G => ECO:0000250

Chain	Residue	Details
A	LEU206-THR238

---

site_id	SWS_FT_FI10
Number of Residues	1
Details	MOD_RES: Pyrrolidone carboxylic acid => ECO:0000250

Chain	Residue	Details
A	GLN1

---

site_id	SWS_FT_FI11
Number of Residues	1
Details	MOD_RES: N6-(retinylidene)lysine => ECO:0000250

Chain	Residue	Details
A	LYS221

---