Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6FTL

Rubisco from Skeletonema marinoi

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000287	molecular_function	magnesium ion binding
A	0004497	molecular_function	monooxygenase activity
A	0009536	cellular_component	plastid
A	0015977	biological_process	carbon fixation
A	0016491	molecular_function	oxidoreductase activity
A	0016829	molecular_function	lyase activity
A	0016984	molecular_function	ribulose-bisphosphate carboxylase activity
A	0019253	biological_process	reductive pentose-phosphate cycle
A	0046872	molecular_function	metal ion binding
C	0000287	molecular_function	magnesium ion binding
C	0004497	molecular_function	monooxygenase activity
C	0009536	cellular_component	plastid
C	0015977	biological_process	carbon fixation
C	0016491	molecular_function	oxidoreductase activity
C	0016829	molecular_function	lyase activity
C	0016984	molecular_function	ribulose-bisphosphate carboxylase activity
C	0019253	biological_process	reductive pentose-phosphate cycle
C	0046872	molecular_function	metal ion binding
E	0000287	molecular_function	magnesium ion binding
E	0004497	molecular_function	monooxygenase activity
E	0009536	cellular_component	plastid
E	0015977	biological_process	carbon fixation
E	0016491	molecular_function	oxidoreductase activity
E	0016829	molecular_function	lyase activity
E	0016984	molecular_function	ribulose-bisphosphate carboxylase activity
E	0019253	biological_process	reductive pentose-phosphate cycle
E	0046872	molecular_function	metal ion binding
G	0000287	molecular_function	magnesium ion binding
G	0004497	molecular_function	monooxygenase activity
G	0009536	cellular_component	plastid
G	0015977	biological_process	carbon fixation
G	0016491	molecular_function	oxidoreductase activity
G	0016829	molecular_function	lyase activity
G	0016984	molecular_function	ribulose-bisphosphate carboxylase activity
G	0019253	biological_process	reductive pentose-phosphate cycle
G	0046872	molecular_function	metal ion binding
I	0009507	cellular_component	chloroplast
I	0015977	biological_process	carbon fixation
I	0015979	biological_process	photosynthesis
I	0016984	molecular_function	ribulose-bisphosphate carboxylase activity
I	0019253	biological_process	reductive pentose-phosphate cycle
J	0009507	cellular_component	chloroplast
J	0015977	biological_process	carbon fixation
J	0015979	biological_process	photosynthesis
J	0016984	molecular_function	ribulose-bisphosphate carboxylase activity
J	0019253	biological_process	reductive pentose-phosphate cycle
K	0009507	cellular_component	chloroplast
K	0015977	biological_process	carbon fixation
K	0015979	biological_process	photosynthesis
K	0016984	molecular_function	ribulose-bisphosphate carboxylase activity
K	0019253	biological_process	reductive pentose-phosphate cycle
L	0009507	cellular_component	chloroplast
L	0015977	biological_process	carbon fixation
L	0015979	biological_process	photosynthesis
L	0016984	molecular_function	ribulose-bisphosphate carboxylase activity
L	0019253	biological_process	reductive pentose-phosphate cycle

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	binding site for residue MG A 500

Chain	Residue
A	LYS181
A	KCX205
A	ASP207
A	GLU208
A	CAP501
E	ASN127

site_id	AC2
Number of Residues	25
Details	binding site for residue CAP A 501

Chain	Residue
A	KCX205
A	ASP207
A	GLU208
A	HIS297
A	ARG298
A	HIS330
A	LYS337
A	LEU338
A	SER382
A	GLY383
A	GLY384
A	GLY406
A	GLY407
A	MG500
A	HOH622
A	HOH625
A	HOH628
E	GLU64
E	THR69
E	TRP70
E	ASN127
E	HOH666
A	THR177
A	LYS179
A	LYS181

site_id	AC3
Number of Residues	7
Details	binding site for residue EDO I 201

Chain	Residue
A	ALA263
A	VAL264
I	GLN120
I	ILE121
I	VAL122
I	TYR123
J	ASP115

site_id	AC4
Number of Residues	4
Details	binding site for residue EDO I 202

Chain	Residue
A	TYR260
G	HOH658
I	GLN120
I	HOH304

site_id	AC5
Number of Residues	6
Details	binding site for residue MG C 501

Chain	Residue
C	LYS179
C	LYS181
C	KCX205
C	ASP207
C	GLU208
C	CAP502

site_id	AC6
Number of Residues	24
Details	binding site for residue CAP C 502

Chain	Residue
C	GLU64
C	THR69
C	TRP70
C	ASN127
C	THR177
C	LYS179
C	LYS181
C	KCX205
C	ASP207
C	GLU208
C	HIS297
C	ARG298
C	HIS330
C	LYS337
C	LEU338
C	SER382
C	GLY383
C	GLY384
C	GLY406
C	GLY407
C	MG501
C	HOH609
C	HOH617
C	HOH631

site_id	AC7
Number of Residues	3
Details	binding site for residue EDO C 503

Chain	Residue
C	TYR260
C	HOH629
J	GLN120

site_id	AC8
Number of Residues	7
Details	binding site for residue EDO J 201

Chain	Residue
C	ALA263
C	VAL264
J	GLN120
J	ILE121
J	VAL122
J	TYR123
K	ASP115

site_id	AC9
Number of Residues	5
Details	binding site for residue EDO J 202

Chain	Residue
I	ILE125
I	LYS126
I	SER127
J	ASP112
J	HOH318

site_id	AD1
Number of Residues	6
Details	binding site for residue EDO J 203

Chain	Residue
J	SER127
J	VAL130
J	HOH301
J	HOH311
K	TYR110
K	ASP112

site_id	AD2
Number of Residues	4
Details	binding site for residue MG E 501

Chain	Residue
E	KCX205
E	ASP207
E	GLU208
E	CAP502

site_id	AD3
Number of Residues	25
Details	binding site for residue CAP E 502

Chain	Residue
A	TRP70
A	ASN127
E	THR177
E	LYS179
E	LYS181
E	KCX205
E	ASP207
E	GLU208
E	HIS297
E	ARG298
E	HIS330
E	LYS337
E	LEU338
E	SER382
E	GLY383
E	GLY384
E	GLY406
E	GLY407
E	MG501
E	HOH609
E	HOH611
E	HOH627
E	HOH658
A	GLU64
A	THR69

site_id	AD4
Number of Residues	5
Details	binding site for residue EDO E 503

Chain	Residue
E	ASP350
E	LEU354
E	GLU358
E	ASN360
E	HOH632

site_id	AD5
Number of Residues	5
Details	binding site for residue EDO E 504

Chain	Residue
E	LYO198
E	GLY199
E	GLN417
E	THR421
E	HOH638

site_id	AD6
Number of Residues	7
Details	binding site for residue EDO K 201

Chain	Residue
E	ALA263
E	VAL264
K	GLN120
K	ILE121
K	VAL122
K	TYR123
L	ASP115

site_id	AD7
Number of Residues	4
Details	binding site for residue EDO K 202

Chain	Residue
E	TYR260
K	GLN120
K	HOH302
K	HOH329

site_id	AD8
Number of Residues	6
Details	binding site for residue EDO K 203

Chain	Residue
K	SER127
K	VAL130
K	HOH303
K	HOH311
L	TYR110
L	ASP112

site_id	AD9
Number of Residues	2
Details	binding site for residue EDO K 204

Chain	Residue
K	ASP13
K	ARG102

site_id	AE1
Number of Residues	5
Details	binding site for residue EDO K 205

Chain	Residue
K	ARG72
K	CYS75
K	ALA76
K	ILE80
K	ASN101

site_id	AE2
Number of Residues	5
Details	binding site for residue MG G 501

Chain	Residue
G	LYS181
G	KCX205
G	ASP207
G	GLU208
G	CAP502

site_id	AE3
Number of Residues	25
Details	binding site for residue CAP G 502

Chain	Residue
G	GLU64
G	THR69
G	TRP70
G	ASN127
G	THR177
G	LYS179
G	LYS181
G	KCX205
G	ASP207
G	GLU208
G	HIS297
G	ARG298
G	HIS330
G	LYS337
G	LEU338
G	SER382
G	GLY383
G	GLY384
G	GLY406
G	GLY407
G	MG501
G	HOH614
G	HOH622
G	HOH642
G	HOH648

site_id	AE4
Number of Residues	6
Details	binding site for residue EDO G 503

Chain	Residue
G	ASP350
G	LEU354
G	LEU357
G	GLU358
G	ASN360
G	HOH653

site_id	AE5
Number of Residues	4
Details	binding site for residue EDO G 504

Chain	Residue
G	TYR277
G	THR303
G	TYR304
G	HOH674

site_id	AE6
Number of Residues	8
Details	binding site for residue EDO L 201

Chain	Residue
G	ALA263
G	VAL264
G	HOH662
I	ASP115
L	GLN120
L	ILE121
L	VAL122
L	TYR123

site_id	AE7
Number of Residues	3
Details	binding site for residue EDO L 202

Chain	Residue
E	HOH603
L	GLN120
L	HOH333

site_id	AE8
Number of Residues	6
Details	binding site for residue EDO L 203

Chain	Residue
I	TYR110
I	ASP112
L	LYS126
L	SER127
L	HOH304
L	HOH326

site_id	AE9
Number of Residues	17
Details	binding site for Di-peptide LEU C 149 and LOH C 150

Chain	Residue
A	CYS109
A	ASP110
A	SER147
A	THR151
C	ILE144
C	PRO145
C	HIS146
C	SER147
C	TYR148
C	THR151
C	PHE152
C	MET323
C	ASP370
C	TRP371
C	ALA372
C	LEU374
E	PRO214

site_id	AF1
Number of Residues	13
Details	binding site for Di-peptide LOH C 150 and THR C 151

Chain	Residue
A	CYS109
A	ASP110
A	SER147
A	LOH150
A	THR151
C	ALA115
C	HIS146
C	SER147
C	TYR148
C	LEU149
C	PHE152
C	ALA372
E	PRO214

site_id	AF2
Number of Residues	15
Details	binding site for Di-peptide LEU C 197 and LYO C 198

Chain	Residue
C	VAL193
C	TYR194
C	GLU195
C	GLY196
C	GLY199
C	GLY200
C	LEU201
C	ASP202
C	LEU204
C	ALA232
C	ALA235
C	LYS240
C	GLY241
C	GLN417
I	GLU49

site_id	AF3
Number of Residues	11
Details	binding site for Di-peptide LYO C 198 and GLY C 199

Chain	Residue
C	TYR194
C	GLU195
C	GLY196
C	LEU197
C	GLY200
C	ALA235
C	GLN417
C	ALA420
C	THR421
I	GLU49
J	PHE10

site_id	AF4
Number of Residues	17
Details	binding site for Di-peptide LEU E 149 and LOH E 150

Chain	Residue
E	ILE144
E	PRO145
E	HIS146
E	SER147
E	TYR148
E	THR151
E	PHE152
E	MET323
E	ASP370
E	ALA372
E	LEU374
G	CYS109
G	GLU114
G	SER147
G	THR151
G	PRO214
G	HOH643

site_id	AF5
Number of Residues	14
Details	binding site for Di-peptide LOH E 150 and THR E 151

Chain	Residue
E	ALA115
E	HIS146
E	SER147
E	TYR148
E	LEU149
E	PHE152
E	ALA372
E	HOH605
G	CYS109
G	GLU114
G	SER147
G	THR151
G	PRO214
G	HOH643

site_id	AF6
Number of Residues	16
Details	binding site for Di-peptide LEU E 197 and LYO E 198

Chain	Residue
E	VAL193
E	TYR194
E	GLU195
E	GLY196
E	GLY199
E	GLY200
E	LEU201
E	ASP202
E	PHE203
E	LEU204
E	ALA232
E	ALA235
E	LYS240
E	GLY241
E	EDO504
J	GLU49

site_id	AF7
Number of Residues	11
Details	binding site for Di-peptide LYO E 198 and GLY E 199

Chain	Residue
E	TYR194
E	GLU195
E	GLY196
E	LEU197
E	GLY200
E	ALA235
E	ALA420
E	THR421
E	EDO504
J	GLU49
K	PHE10

site_id	AF8
Number of Residues	14
Details	binding site for Di-peptide LEU G 149 and LOH G 150

Chain	Residue
A	PRO214
E	ASP110
E	SER147
G	ILE144
G	PRO145
G	HIS146
G	SER147
G	TYR148
G	THR151
G	PHE152
G	MET323
G	ASP370
G	ALA372
G	LEU374

site_id	AF9
Number of Residues	12
Details	binding site for Di-peptide LOH G 150 and THR G 151

Chain	Residue
A	PRO214
E	ASP110
E	SER147
E	LOH150
G	ALA115
G	HIS146
G	SER147
G	TYR148
G	LEU149
G	PHE152
G	ALA372
G	HOH611

site_id	AG1
Number of Residues	15
Details	binding site for Di-peptide LEU G 197 and LYO G 198

Chain	Residue
G	VAL193
G	TYR194
G	GLU195
G	GLY196
G	GLY199
G	GLY200
G	LEU201
G	ASP202
G	LEU204
G	ILE229
G	ALA232
G	ALA235
G	LYS240
G	GLY241
K	GLU49

site_id	AG2
Number of Residues	11
Details	binding site for Di-peptide LYO G 198 and GLY G 199

Chain	Residue
G	TYR194
G	GLU195
G	GLY196
G	LEU197
G	GLY200
G	ALA235
G	GLN417
G	ALA420
G	THR421
K	GLU49
L	PHE10

Functional Information from PROSITE/UniProt

site_id	PS00157
Number of Residues	9
Details	RUBISCO_LARGE Ribulose bisphosphate carboxylase large chain active site. GlDFlKdDE

Chain	Residue	Details
A	GLY200-GLU208

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)