Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1RXO

ACTIVATED SPINACH RUBISCO IN COMPLEX WITH ITS SUBSTRATE RIBULOSE-1,5-BISPHOSPHATE AND CALCIUM

Functional Information from GO Data

Chain	GOid	namespace	contents
B	0000287	molecular_function	magnesium ion binding
B	0004497	molecular_function	monooxygenase activity
B	0009507	cellular_component	chloroplast
B	0009853	biological_process	photorespiration
B	0015977	biological_process	carbon fixation
B	0015979	biological_process	photosynthesis
B	0016829	molecular_function	lyase activity
B	0016984	molecular_function	ribulose-bisphosphate carboxylase activity
B	0019253	biological_process	reductive pentose-phosphate cycle
B	0046872	molecular_function	metal ion binding
C	0009507	cellular_component	chloroplast
C	0009853	biological_process	photorespiration
C	0015977	biological_process	carbon fixation
C	0015979	biological_process	photosynthesis
C	0016984	molecular_function	ribulose-bisphosphate carboxylase activity
C	0019253	biological_process	reductive pentose-phosphate cycle
E	0000287	molecular_function	magnesium ion binding
E	0004497	molecular_function	monooxygenase activity
E	0009507	cellular_component	chloroplast
E	0009853	biological_process	photorespiration
E	0015977	biological_process	carbon fixation
E	0015979	biological_process	photosynthesis
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
F	0009507	cellular_component	chloroplast
F	0009853	biological_process	photorespiration
F	0015977	biological_process	carbon fixation
F	0015979	biological_process	photosynthesis
F	0016984	molecular_function	ribulose-bisphosphate carboxylase activity
F	0019253	biological_process	reductive pentose-phosphate cycle
H	0000287	molecular_function	magnesium ion binding
H	0004497	molecular_function	monooxygenase activity
H	0009507	cellular_component	chloroplast
H	0009853	biological_process	photorespiration
H	0015977	biological_process	carbon fixation
H	0015979	biological_process	photosynthesis
H	0016829	molecular_function	lyase activity
H	0016984	molecular_function	ribulose-bisphosphate carboxylase activity
H	0019253	biological_process	reductive pentose-phosphate cycle
H	0046872	molecular_function	metal ion binding
I	0009507	cellular_component	chloroplast
I	0009853	biological_process	photorespiration
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
L	0000287	molecular_function	magnesium ion binding
L	0004497	molecular_function	monooxygenase activity
L	0009507	cellular_component	chloroplast
L	0009853	biological_process	photorespiration
L	0015977	biological_process	carbon fixation
L	0015979	biological_process	photosynthesis
L	0016829	molecular_function	lyase activity
L	0016984	molecular_function	ribulose-bisphosphate carboxylase activity
L	0019253	biological_process	reductive pentose-phosphate cycle
L	0046872	molecular_function	metal ion binding
S	0009507	cellular_component	chloroplast
S	0009853	biological_process	photorespiration
S	0015977	biological_process	carbon fixation
S	0015979	biological_process	photosynthesis
S	0016984	molecular_function	ribulose-bisphosphate carboxylase activity
S	0019253	biological_process	reductive pentose-phosphate cycle

Functional Information from PDB Data

site_id	AC1
Number of Residues	21
Details	BINDING SITE FOR RESIDUE RUB L 476

Chain	Residue
E	TRP66
L	LYS175
L	KCX201
L	GLU204
L	HIS294
L	ARG295
L	HIS298
L	SER379
L	GLY380
L	GLY381
L	GLY403
L	GLY404
L	CA477
L	HOH525
L	HOH526
L	HOH541
L	HOH562
L	HOH568
L	HOH593
L	HOH619
L	HOH660

site_id	AC2
Number of Residues	21
Details	BINDING SITE FOR RESIDUE RUB B 476

Chain	Residue
B	TRP66
B	LYS175
B	KCX201
B	GLU204
B	HIS294
B	ARG295
B	HIS298
B	SER379
B	GLY380
B	GLY381
B	GLY403
B	GLY404
B	CA477
B	HOH526
B	HOH527
B	HOH542
B	HOH563
B	HOH569
B	HOH594
B	HOH620
B	HOH661

site_id	AC3
Number of Residues	21
Details	BINDING SITE FOR RESIDUE RUB E 476

Chain	Residue
E	LYS175
E	KCX201
E	GLU204
E	HIS294
E	ARG295
E	HIS298
E	SER379
E	GLY380
E	GLY381
E	GLY403
E	GLY404
E	CA477
E	HOH566
E	HOH567
E	HOH583
E	HOH606
E	HOH613
E	HOH638
E	HOH665
E	HOH709
L	TRP66

site_id	AC4
Number of Residues	21
Details	BINDING SITE FOR RESIDUE RUB H 476

Chain	Residue
H	TRP66
H	LYS175
H	KCX201
H	GLU204
H	HIS294
H	ARG295
H	HIS298
H	SER379
H	GLY380
H	GLY381
H	GLY403
H	GLY404
H	CA477
H	HOH528
H	HOH529
H	HOH544
H	HOH565
H	HOH571
H	HOH596
H	HOH622
H	HOH663

site_id	AC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA L 477

Chain	Residue
L	RUB476
L	HOH583
L	KCX201
L	ASP203
L	GLU204

site_id	AC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA B 477

Chain	Residue
B	KCX201
B	ASP203
B	GLU204
B	RUB476
B	HOH584

site_id	AC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA E 477

Chain	Residue
E	KCX201
E	ASP203
E	GLU204
E	RUB476
E	HOH628

site_id	AC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA H 477

Chain	Residue
H	KCX201
H	ASP203
H	GLU204
H	RUB476
H	HOH586

site_id	ACB
Number of Residues	3
Details	ACTIVE SITE.

Chain	Residue
B	KCX201
B	ASP203
B	GLU204

site_id	ACE
Number of Residues	3
Details	ACTIVE SITE.

Chain	Residue
E	KCX201
E	ASP203
E	GLU204

site_id	ACH
Number of Residues	3
Details	ACTIVE SITE.

Chain	Residue
H	KCX201
H	ASP203
H	GLU204

site_id	ACL
Number of Residues	3
Details	ACTIVE SITE.

Chain	Residue
L	KCX201
L	ASP203
L	GLU204

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
L	GLY196-GLU204

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	ACT_SITE: Proton acceptor => ECO:0000269\|PubMed:2118958, ECO:0000269\|PubMed:637859, ECO:0000305\|PubMed:9092835

Chain	Residue	Details
L	LYS175
B	LYS175
E	LYS175
H	LYS175

site_id	SWS_FT_FI2
Number of Residues	4
Details	ACT_SITE: Proton acceptor => ECO:0000269\|PubMed:637859

Chain	Residue	Details
L	HIS294
B	HIS294
E	HIS294
H	HIS294

site_id	SWS_FT_FI3
Number of Residues	20
Details	BINDING: BINDING => ECO:0000269\|PubMed:9034362, ECO:0007744\|PDB:1RCX

Chain	Residue	Details
L	THR65
B	LYS334
E	THR65
E	GLU204
E	HIS294
E	HIS327
E	LYS334
H	THR65
H	GLU204
H	HIS294
H	HIS327
L	GLU204
H	LYS334
L	HIS294
L	HIS327
L	LYS334
B	THR65
B	GLU204
B	HIS294
B	HIS327

site_id	SWS_FT_FI4
Number of Residues	4
Details	BINDING: in homodimeric partner => ECO:0000269\|PubMed:9034362, ECO:0007744\|PDB:1RCX

Chain	Residue	Details
L	ASN123
B	ASN123
E	ASN123
H	ASN123

site_id	SWS_FT_FI5
Number of Residues	12
Details	BINDING:

Chain	Residue	Details
L	THR173
H	THR173
H	LYS177
H	SER379
L	LYS177
L	SER379
B	THR173
B	LYS177
B	SER379
E	THR173
E	LYS177
E	SER379

site_id	SWS_FT_FI6
Number of Residues	4
Details	BINDING: via carbamate group => ECO:0000269\|PubMed:8648644, ECO:0000269\|PubMed:9092835, ECO:0000305\|PubMed:14596800, ECO:0000305\|PubMed:2118958, ECO:0000305\|PubMed:9034362

Chain	Residue	Details
L	KCX201
B	KCX201
E	KCX201
H	KCX201

site_id	SWS_FT_FI7
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269\|PubMed:8648644, ECO:0000269\|PubMed:9092835, ECO:0000305\|PubMed:14596800, ECO:0000305\|PubMed:2118958, ECO:0000305\|PubMed:9034362

Chain	Residue	Details
L	ASP203
B	ASP203
E	ASP203
H	ASP203

site_id	SWS_FT_FI8
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269\|PubMed:9034362, ECO:0007744\|PDB:1RXO

Chain	Residue	Details
L	ARG295
B	ARG295
E	ARG295
H	ARG295

site_id	SWS_FT_FI9
Number of Residues	12
Details	BINDING: BINDING => ECO:0000269\|PubMed:9034362, ECO:0007744\|PDB:1RCX, ECO:0007744\|PDB:1RXO

Chain	Residue	Details
L	GLY381
H	GLY381
H	GLY403
H	GLY404
L	GLY403
L	GLY404
B	GLY381
B	GLY403
B	GLY404
E	GLY381
E	GLY403
E	GLY404

site_id	SWS_FT_FI10
Number of Residues	4
Details	SITE: Not N6-methylated => ECO:0000269\|PubMed:2928307

Chain	Residue	Details
L	LYS14
B	LYS14
E	LYS14
H	LYS14

site_id	SWS_FT_FI11
Number of Residues	4
Details	SITE: Transition state stabilizer => ECO:0000305\|PubMed:8955130

Chain	Residue	Details
L	LYS334
B	LYS334
E	LYS334
H	LYS334

site_id	SWS_FT_FI12
Number of Residues	4
Details	MOD_RES: N-acetylproline => ECO:0000269\|PubMed:2928307

Chain	Residue	Details
L	PRO3
B	PRO3
E	PRO3
H	PRO3

site_id	SWS_FT_FI13
Number of Residues	4
Details	MOD_RES: N6-carboxylysine => ECO:0000269\|PubMed:14596800, ECO:0000269\|PubMed:2118958, ECO:0000269\|PubMed:8648644, ECO:0000269\|PubMed:9034362, ECO:0000269\|PubMed:9092835

Chain	Residue	Details
L	KCX201
B	KCX201
E	KCX201
H	KCX201

Catalytic Information from CSA

site_id	CSA1
Number of Residues	5
Details	Annotated By Reference To The Literature 1rbl

Chain	Residue	Details
L	LYS175
L	HIS294
L	LYS177
L	ASP203
L	HIS327

site_id	CSA2
Number of Residues	5
Details	Annotated By Reference To The Literature 1rbl

Chain	Residue	Details
B	LYS175
B	HIS294
B	LYS177
B	ASP203
B	HIS327

site_id	CSA3
Number of Residues	5
Details	Annotated By Reference To The Literature 1rbl

Chain	Residue	Details
E	LYS175
E	HIS294
E	LYS177
E	ASP203
E	HIS327

site_id	CSA4
Number of Residues	5
Details	Annotated By Reference To The Literature 1rbl

Chain	Residue	Details
H	LYS175
H	HIS294
H	LYS177
H	ASP203
H	HIS327

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