3T45

Crystal structure of bacteriorhodopsin mutant A215T, a phototaxis signaling mutant at 3.0 A resolution

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005216	molecular_function	monoatomic ion channel activity
A	0006811	biological_process	monoatomic ion transport
A	0016020	cellular_component	membrane
B	0005216	molecular_function	monoatomic ion channel activity
B	0006811	biological_process	monoatomic ion transport
B	0016020	cellular_component	membrane
C	0005216	molecular_function	monoatomic ion channel activity
C	0006811	biological_process	monoatomic ion transport
C	0016020	cellular_component	membrane

Functional Information from PDB Data

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

Chain	Residue
A	TRP86
A	PRO186
A	TRP189
A	LYS216
A	THR90
A	LEU93
A	MET118
A	TRP138
A	SER141
A	THR142
A	TRP182
A	TYR185

---

site_id	AC2
Number of Residues	13
Details	BINDING SITE FOR RESIDUE RET B 301

Chain	Residue
B	TRP86
B	THR90
B	LEU93
B	MET118
B	TRP138
B	SER141
B	THR142
B	TRP182
B	TYR185
B	PRO186
B	TRP189
B	ASP212
B	LYS216

---

site_id	AC3
Number of Residues	13
Details	BINDING SITE FOR RESIDUE RET C 301

Chain	Residue
C	TRP86
C	THR90
C	LEU93
C	MET118
C	TRP138
C	SER141
C	THR142
C	TRP182
C	TYR185
C	PRO186
C	TRP189
C	ASP212
C	LYS216

---

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE LI1 A 600

Chain	Residue
A	PHE135
A	LEU190
A	ALA196
B	TRP12
B	ILE203

---

site_id	AC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE LI1 B 602

Chain	Residue
A	TYR64
B	GLY113
B	GLY116
B	ILE117

---

site_id	AC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE LI1 B 603

Chain	Residue
A	LEU15
B	LEU25
B	LEU58
C	ALA139
C	ILE140
C	LI1606

---

site_id	AC7
Number of Residues	12
Details	BINDING SITE FOR RESIDUE LI1 B 604

Chain	Residue
A	LI1608
B	TYR64
B	TRP80
B	PHE88
B	LI1615
C	THR67
C	TRP80
C	ALA84
C	GLY116
C	GLY120
C	LEU123
C	LYS129

---

site_id	AC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE LI1 B 605

Chain	Residue
B	LEU28
B	LYS40
B	ALA44
C	TYR147

---

site_id	AC9
Number of Residues	7
Details	BINDING SITE FOR RESIDUE LI1 C 606

Chain	Residue
A	TRP12
A	GLY73
A	GLN75
A	ASN202
A	ILE203
B	LI1603
C	LEU190

---

site_id	BC1
Number of Residues	2
Details	BINDING SITE FOR RESIDUE LI1 B 615

Chain	Residue
B	TRP80
B	LI1604

---

site_id	BC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE LI1 B 611

Chain	Residue
B	TYR131
B	LEU190
B	LI1612
C	TRP12
C	ASN202
C	ILE203

---

site_id	BC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE LI1 B 612

Chain	Residue
B	LI1611
C	VAL199
C	PRO200

---

site_id	BC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE LI1 C 613

Chain	Residue
A	ILE117
A	TYR147
C	LEU25
C	LEU28
C	GLY31
C	PHE54

---

site_id	BC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE LI1 A 608

Chain	Residue
A	GLY116
A	LEU127
B	LI1604
C	MET56
C	TYR64

---

Functional Information from PROSITE/UniProt

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

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	57
Details	TRANSMEM: Helical; Name=Helix A => ECO:0000269|PubMed:10452895, ECO:0000269|PubMed:28008064, ECO:0007744|PDB:1C3W

Chain	Residue	Details
A	TRP10-VAL29
B	TRP10-VAL29
C	TRP10-VAL29

---

site_id	SWS_FT_FI2
Number of Residues	120
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
B	LYS30-TYR43
B	LEU97-THR107
B	GLY155-LYS172
C	LYS30-TYR43
C	LEU97-THR107
C	GLY155-LYS172

---

site_id	SWS_FT_FI3
Number of Residues	54
Details	TRANSMEM: Helical; Name=Helix B => ECO:0000269|PubMed:10452895, ECO:0000269|PubMed:28008064, ECO:0007744|PDB:1C3W

Chain	Residue	Details
A	ALA44-LEU62
B	ALA44-LEU62
C	ALA44-LEU62

---

site_id	SWS_FT_FI4
Number of Residues	99
Details	TOPO_DOM: Extracellular => ECO:0000269|PubMed:10452895, ECO:0000269|PubMed:28008064, ECO:0007744|PDB:1C3W

Chain	Residue	Details
A	GLY63-TYR79
A	THR128-ARG134
A	GLY192-ILE203
B	GLY63-TYR79
B	THR128-ARG134
B	GLY192-ILE203
C	GLY63-TYR79
C	THR128-ARG134
C	GLY192-ILE203

---

site_id	SWS_FT_FI5
Number of Residues	48
Details	TRANSMEM: Helical; Name=Helix C => ECO:0000269|PubMed:10452895, ECO:0000269|PubMed:28008064, ECO:0007744|PDB:1C3W

Chain	Residue	Details
A	TRP80-ASP96
B	TRP80-ASP96
C	TRP80-ASP96

---

site_id	SWS_FT_FI6
Number of Residues	57
Details	TRANSMEM: Helical; Name=Helix D => ECO:0000269|PubMed:10452895, ECO:0000269|PubMed:28008064, ECO:0007744|PDB:1C3W

Chain	Residue	Details
A	ILE108-LEU127
B	ILE108-LEU127
C	ILE108-LEU127

---

site_id	SWS_FT_FI7
Number of Residues	57
Details	TRANSMEM: Helical; Name=Helix E => ECO:0000269|PubMed:10452895, ECO:0000269|PubMed:28008064, ECO:0007744|PDB:1C3W

Chain	Residue	Details
A	PHE135-PHE154
B	PHE135-PHE154
C	PHE135-PHE154

---

site_id	SWS_FT_FI8
Number of Residues	54
Details	TRANSMEM: Helical; Name=Helix F => ECO:0000269|PubMed:10452895, ECO:0000269|PubMed:28008064, ECO:0007744|PDB:1C3W

Chain	Residue	Details
A	VAL173-ILE191
B	VAL173-ILE191
C	VAL173-ILE191

---

site_id	SWS_FT_FI9
Number of Residues	57
Details	TRANSMEM: Helical; Name=Helix G => ECO:0000269|PubMed:10452895, ECO:0000269|PubMed:28008064, ECO:0007744|PDB:1C3W

Chain	Residue	Details
A	GLU204-LEU223
B	GLU204-LEU223
C	GLU204-LEU223

---

site_id	SWS_FT_FI10
Number of Residues	3
Details	SITE: Primary proton acceptor => ECO:0000305|PubMed:10903866, ECO:0000305|PubMed:10949309, ECO:0000305|PubMed:28008064

Chain	Residue	Details
A	ASP85
B	ASP85
C	ASP85

---

site_id	SWS_FT_FI11
Number of Residues	3
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
B	LYS216
C	LYS216

---