Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

8RUC

ACTIVATED SPINACH RUBISCO COMPLEXED WITH 2-CARBOXYARABINITOL BISPHOSPHATE

Replaces: 8RUB

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000287	molecular_function	magnesium ion binding
A	0004497	molecular_function	monooxygenase activity
A	0009507	cellular_component	chloroplast
A	0009853	biological_process	photorespiration
A	0015977	biological_process	carbon fixation
A	0015979	biological_process	photosynthesis
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	0009507	cellular_component	chloroplast
C	0009853	biological_process	photorespiration
C	0015977	biological_process	carbon fixation
C	0015979	biological_process	photosynthesis
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	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
G	0000287	molecular_function	magnesium ion binding
G	0004497	molecular_function	monooxygenase activity
G	0009507	cellular_component	chloroplast
G	0009853	biological_process	photorespiration
G	0015977	biological_process	carbon fixation
G	0015979	biological_process	photosynthesis
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	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
J	0009507	cellular_component	chloroplast
J	0009853	biological_process	photorespiration
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	0009853	biological_process	photorespiration
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	0009853	biological_process	photorespiration
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	4
Details	BINDING SITE FOR RESIDUE MG A 476

Chain	Residue
A	KCX201
A	ASP203
A	GLU204
A	CAP477

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG C 476

Chain	Residue
C	KCX201
C	ASP203
C	GLU204
C	CAP477

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG E 476

Chain	Residue
E	KCX201
E	ASP203
E	GLU204
E	CAP477

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG G 476

Chain	Residue
G	KCX201
G	ASP203
G	GLU204
G	CAP477

site_id	AC5
Number of Residues	29
Details	BINDING SITE FOR RESIDUE CAP A 477

Chain	Residue
A	THR173
A	LYS175
A	LYS177
A	KCX201
A	ASP203
A	GLU204
A	HIS294
A	ARG295
A	HIS327
A	LYS334
A	LEU335
A	SER379
A	GLY380
A	GLY381
A	GLY403
A	GLY404
A	MG476
A	HOH483
A	HOH511
A	HOH621
A	HOH625
A	HOH673
A	HOH739
A	HOH748
E	GLU60
E	THR65
E	TRP66
E	ASN123
E	HOH612

site_id	AC6
Number of Residues	29
Details	BINDING SITE FOR RESIDUE CAP C 477

Chain	Residue
C	GLU60
C	THR65
C	TRP66
C	ASN123
C	THR173
C	LYS175
C	LYS177
C	KCX201
C	ASP203
C	GLU204
C	HIS294
C	ARG295
C	HIS327
C	LYS334
C	LEU335
C	SER379
C	GLY380
C	GLY381
C	GLY403
C	GLY404
C	MG476
C	HOH495
C	HOH505
C	HOH546
C	HOH663
C	HOH664
C	HOH722
C	HOH723
C	HOH752

site_id	AC7
Number of Residues	28
Details	BINDING SITE FOR RESIDUE CAP E 477

Chain	Residue
E	GLU204
E	HIS294
E	ARG295
E	HIS327
E	LYS334
E	LEU335
E	SER379
E	GLY380
E	GLY381
E	GLY403
E	GLY404
E	MG476
E	HOH479
E	HOH492
E	HOH502
E	HOH662
E	HOH666
E	HOH668
E	HOH722
A	GLU60
A	THR65
A	TRP66
A	ASN123
E	THR173
E	LYS175
E	LYS177
E	KCX201
E	ASP203

site_id	AC8
Number of Residues	30
Details	BINDING SITE FOR RESIDUE CAP G 477

Chain	Residue
G	GLU60
G	THR65
G	TRP66
G	ASN123
G	THR173
G	LYS175
G	LYS177
G	KCX201
G	ASP203
G	GLU204
G	HIS294
G	ARG295
G	HIS327
G	LYS334
G	LEU335
G	SER379
G	GLY380
G	GLY381
G	GLY403
G	GLY404
G	MG476
G	HOH480
G	HOH495
G	HOH617
G	HOH682
G	HOH683
G	HOH692
G	HOH712
G	HOH729
G	HOH732

site_id	ACA
Number of Residues	4
Details	CATALYTIC RESIDUES

Chain	Residue
A	KCX201
A	ASP203
A	GLU204
A	MG476

site_id	ACC
Number of Residues	4
Details	CATALYTIC RESIDUES

Chain	Residue
C	KCX201
C	ASP203
C	GLU204
C	MG476

site_id	ACE
Number of Residues	4
Details	CATALYTIC RESIDUES

Chain	Residue
E	ASP203
E	GLU204
E	MG476
E	KCX201

site_id	ACG
Number of Residues	4
Details	CATALYTIC RESIDUES

Chain	Residue
G	KCX201
G	ASP203
G	GLU204
G	MG476

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
A	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
A	LYS175
C	LYS175
E	LYS175
G	LYS175

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

Chain	Residue	Details
A	HIS294
C	HIS294
E	HIS294
G	HIS294

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

Chain	Residue	Details
A	THR65
C	LYS334
E	THR65
E	GLU204
E	HIS294
E	HIS327
E	LYS334
G	THR65
G	GLU204
G	HIS294
G	HIS327
A	GLU204
G	LYS334
A	HIS294
A	HIS327
A	LYS334
C	THR65
C	GLU204
C	HIS294
C	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
A	ASN123
C	ASN123
E	ASN123
G	ASN123

site_id	SWS_FT_FI5
Number of Residues	12
Details	BINDING:

Chain	Residue	Details
A	THR173
G	THR173
G	LYS177
G	SER379
A	LYS177
A	SER379
C	THR173
C	LYS177
C	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
A	KCX201
C	KCX201
E	KCX201
G	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
A	ASP203
C	ASP203
E	ASP203
G	ASP203

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

Chain	Residue	Details
A	ARG295
C	ARG295
E	ARG295
G	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
A	GLY381
G	GLY381
G	GLY403
G	GLY404
A	GLY403
A	GLY404
C	GLY381
C	GLY403
C	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
A	LYS14
C	LYS14
E	LYS14
G	LYS14

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

Chain	Residue	Details
A	LYS334
C	LYS334
E	LYS334
G	LYS334

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

Chain	Residue	Details
A	PRO3
C	PRO3
E	PRO3
G	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
A	KCX201
C	KCX201
E	KCX201
G	KCX201

Catalytic Information from CSA

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

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

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

Chain	Residue	Details
C	LYS175
C	HIS294
C	LYS177
C	ASP203
C	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
G	LYS175
G	HIS294
G	LYS177
G	ASP203
G	HIS327

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