Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1RZH

PHOTOSYNTHETIC REACTION CENTER DOUBLE MUTANT FROM RHODOBACTER SPHAEROIDES WITH ASP L213 REPLACED WITH ASN AND ARG M233 REPLACED WITH CYS IN THE CHARGE-NEUTRAL DQAQB STATE (TRIGONAL FORM)

Functional Information from GO Data

Chain	GOid	namespace	contents
H	0015979	biological_process	photosynthesis
H	0016168	molecular_function	chlorophyll binding
H	0019684	biological_process	photosynthesis, light reaction
H	0030077	cellular_component	plasma membrane light-harvesting complex
H	0042314	molecular_function	bacteriochlorophyll binding
H	0042717	cellular_component	plasma membrane-derived chromatophore membrane
L	0009772	biological_process	photosynthetic electron transport in photosystem II
L	0015979	biological_process	photosynthesis
L	0016168	molecular_function	chlorophyll binding
L	0019684	biological_process	photosynthesis, light reaction
L	0030077	cellular_component	plasma membrane light-harvesting complex
L	0042314	molecular_function	bacteriochlorophyll binding
L	0042717	cellular_component	plasma membrane-derived chromatophore membrane
L	0046872	molecular_function	metal ion binding
M	0009772	biological_process	photosynthetic electron transport in photosystem II
M	0015979	biological_process	photosynthesis
M	0016168	molecular_function	chlorophyll binding
M	0019684	biological_process	photosynthesis, light reaction
M	0030077	cellular_component	plasma membrane light-harvesting complex
M	0042314	molecular_function	bacteriochlorophyll binding
M	0042717	cellular_component	plasma membrane-derived chromatophore membrane
M	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	21
Details	BINDING SITE FOR RESIDUE BCL L 852

Chain	Residue
L	PHE97
L	HIS168
L	HIS173
L	ILE177
L	PHE180
L	SER244
L	CYS247
L	MET248
L	BCL854
L	BPH856
M	TYR210
L	ALA124
M	BCL851
M	BCL853
L	ALA127
L	LEU131
L	TRP156
L	VAL157
L	THR160
L	TYR162
L	ASN166

site_id	AC2
Number of Residues	15
Details	BINDING SITE FOR RESIDUE BCL L 854

Chain	Residue
L	TYR128
L	ILE150
L	HIS153
L	LEU154
L	BCL852
L	BPH856
L	HOH875
M	PHE197
M	GLY203
M	ILE206
M	ALA207
M	TYR210
M	LEU214
M	U10858
M	LDA861

site_id	AC3
Number of Residues	18
Details	BINDING SITE FOR RESIDUE BPH L 856

Chain	Residue
L	ALA93
L	PHE97
L	TRP100
L	GLU104
L	ILE117
L	ALA120
L	PHE121
L	PHE123
L	ALA124
L	HIS153
L	VAL241
L	BCL852
L	BCL854
M	TYR210
M	ALA213
M	LEU214
M	TRP252
M	MET256

site_id	AC4
Number of Residues	14
Details	BINDING SITE FOR RESIDUE U10 L 859

Chain	Residue
L	ALA186
L	LEU189
L	HIS190
L	LEU193
L	PHE216
L	VAL220
L	TYR222
L	SER223
L	ILE224
L	ILE229
L	HOH988
L	HOH989
L	HOH990
M	TRP129

site_id	AC5
Number of Residues	3
Details	BINDING SITE FOR RESIDUE HTO L 865

Chain	Residue
L	ALA101
L	PRO118
L	PHE119

site_id	AC6
Number of Residues	3
Details	BINDING SITE FOR RESIDUE HTO L 866

Chain	Residue
H	LDA862
L	PHE29
M	GLY257

site_id	AC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE FE2 M 857

Chain	Residue
L	HIS190
L	HIS230
M	HIS219
M	GLU234
M	HIS266

site_id	AC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PO4 M 864

Chain	Residue
M	ASN28
M	GLY53
M	SER54
M	HOH964
M	HOH1000

site_id	AC9
Number of Residues	16
Details	BINDING SITE FOR RESIDUE BCL M 851

Chain	Residue
M	SPO860
L	HIS168
L	MET174
L	ILE177
L	SER178
L	THR182
L	BCL852
L	HOH877
M	MET122
M	TRP157
M	ILE179
M	HIS182
M	LEU183
M	THR186
M	BCL853
M	BPH855

site_id	BC1
Number of Residues	20
Details	BINDING SITE FOR RESIDUE BCL M 853

Chain	Residue
L	TYR162
L	BCL852
M	ALA153
M	LEU156
M	LEU160
M	THR186
M	ASN187
M	PHE189
M	SER190
M	LEU196
M	PHE197
M	HIS202
M	SER205
M	ILE206
M	TYR210
M	VAL276
M	GLY280
M	ILE284
M	BCL851
M	BPH855

site_id	BC2
Number of Residues	18
Details	BINDING SITE FOR RESIDUE BPH M 855

Chain	Residue
L	PHE181
L	ALA184
L	LEU185
L	LEU189
M	LEU60
M	GLY63
M	LEU64
M	PHE67
M	ALA125
M	TRP129
M	THR146
M	ALA149
M	PHE150
M	ALA153
M	ALA273
M	THR277
M	BCL851
M	BCL853

site_id	BC3
Number of Residues	18
Details	BINDING SITE FOR RESIDUE U10 M 858

Chain	Residue
L	PHE29
L	VAL31
L	GLY35
L	PHE39
L	BCL854
M	HIS219
M	THR222
M	ALA248
M	ALA249
M	TRP252
M	MET256
M	PHE258
M	ASN259
M	ALA260
M	THR261
M	ILE265
M	TRP268
M	MET272

site_id	BC4
Number of Residues	17
Details	BINDING SITE FOR RESIDUE SPO M 860

Chain	Residue
M	PHE67
M	PHE68
M	ILE70
M	GLY71
M	TRP75
M	PHE85
M	SER119
M	TRP157
M	LEU160
M	GLY161
M	PHE162
M	TRP171
M	VAL175
M	TYR177
M	GLY178
M	HIS182
M	BCL851

site_id	BC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE LDA M 861

Chain	Residue
L	BCL854
M	PRO200
M	GLY203
M	ALA207
M	PHE208
M	TRP268

site_id	BC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE LDA M 863

Chain	Residue
M	PHE7
M	LEU38
M	LEU39
M	TRP41
M	PHE42

site_id	BC7
Number of Residues	12
Details	BINDING SITE FOR RESIDUE CDL M 900

Chain	Residue
H	TYR30
H	HOH898
L	ASN199
L	HOH982
M	GLY143
M	LYS144
M	HIS145
M	TRP148
M	ARG267
M	TRP271
M	HOH931
M	HOH979

site_id	BC8
Number of Residues	2
Details	BINDING SITE FOR RESIDUE GOL M 867

Chain	Residue
L	TRP266
M	PHE90

site_id	BC9
Number of Residues	5
Details	BINDING SITE FOR RESIDUE LDA H 862

Chain	Residue
H	GLN32
H	TYR40
H	HOH1057
L	HTO866
M	ARG253

Functional Information from PROSITE/UniProt

site_id	PS00244
Number of Residues	27
Details	REACTION_CENTER Photosynthetic reaction center proteins signature. NlfynPfHglSiaflygsallfAmHGA

Chain	Residue	Details
M	ASN195-ALA221
L	ASN166-ALA192

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	58
Details	Topological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"1645718","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	278
Details	Transmembrane: {"description":"Helical"}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	87
Details	Topological domain: {"description":"Periplasmic","evidences":[{"source":"PubMed","id":"1645718","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details