Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

8IO2

The Rubisco assembly intermidate of Arabidopsis thaliana Rubisco accumulation factor 1 (AtRaf1) and Rubisco large subunit (RbcL)

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000287	molecular_function	magnesium ion binding
A	0004497	molecular_function	monooxygenase activity
A	0005515	molecular_function	protein binding
A	0009853	biological_process	photorespiration
A	0015977	biological_process	carbon fixation
A	0015979	biological_process	photosynthesis
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	0031469	cellular_component	bacterial microcompartment
A	0031470	cellular_component	carboxysome
A	0046872	molecular_function	metal ion binding
B	0000287	molecular_function	magnesium ion binding
B	0004497	molecular_function	monooxygenase activity
B	0005515	molecular_function	protein binding
B	0009853	biological_process	photorespiration
B	0015977	biological_process	carbon fixation
B	0015979	biological_process	photosynthesis
B	0016491	molecular_function	oxidoreductase activity
B	0016829	molecular_function	lyase activity
B	0016984	molecular_function	ribulose-bisphosphate carboxylase activity
B	0019253	biological_process	reductive pentose-phosphate cycle
B	0031469	cellular_component	bacterial microcompartment
B	0031470	cellular_component	carboxysome
B	0046872	molecular_function	metal ion binding
C	0000287	molecular_function	magnesium ion binding
C	0004497	molecular_function	monooxygenase activity
C	0005515	molecular_function	protein binding
C	0009853	biological_process	photorespiration
C	0015977	biological_process	carbon fixation
C	0015979	biological_process	photosynthesis
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	0031469	cellular_component	bacterial microcompartment
C	0031470	cellular_component	carboxysome
C	0046872	molecular_function	metal ion binding
D	0000287	molecular_function	magnesium ion binding
D	0004497	molecular_function	monooxygenase activity
D	0005515	molecular_function	protein binding
D	0009853	biological_process	photorespiration
D	0015977	biological_process	carbon fixation
D	0015979	biological_process	photosynthesis
D	0016491	molecular_function	oxidoreductase activity
D	0016829	molecular_function	lyase activity
D	0016984	molecular_function	ribulose-bisphosphate carboxylase activity
D	0019253	biological_process	reductive pentose-phosphate cycle
D	0031469	cellular_component	bacterial microcompartment
D	0031470	cellular_component	carboxysome
D	0046872	molecular_function	metal ion binding
E	0000287	molecular_function	magnesium ion binding
E	0004497	molecular_function	monooxygenase activity
E	0005515	molecular_function	protein binding
E	0009853	biological_process	photorespiration
E	0015977	biological_process	carbon fixation
E	0015979	biological_process	photosynthesis
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	0031469	cellular_component	bacterial microcompartment
E	0031470	cellular_component	carboxysome
E	0046872	molecular_function	metal ion binding
F	0000287	molecular_function	magnesium ion binding
F	0004497	molecular_function	monooxygenase activity
F	0005515	molecular_function	protein binding
F	0009853	biological_process	photorespiration
F	0015977	biological_process	carbon fixation
F	0015979	biological_process	photosynthesis
F	0016491	molecular_function	oxidoreductase activity
F	0016829	molecular_function	lyase activity
F	0016984	molecular_function	ribulose-bisphosphate carboxylase activity
F	0019253	biological_process	reductive pentose-phosphate cycle
F	0031469	cellular_component	bacterial microcompartment
F	0031470	cellular_component	carboxysome
F	0046872	molecular_function	metal ion binding
G	0000287	molecular_function	magnesium ion binding
G	0004497	molecular_function	monooxygenase activity
G	0005515	molecular_function	protein binding
G	0009853	biological_process	photorespiration
G	0015977	biological_process	carbon fixation
G	0015979	biological_process	photosynthesis
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	0031469	cellular_component	bacterial microcompartment
G	0031470	cellular_component	carboxysome
G	0046872	molecular_function	metal ion binding
H	0000287	molecular_function	magnesium ion binding
H	0004497	molecular_function	monooxygenase activity
H	0005515	molecular_function	protein binding
H	0009853	biological_process	photorespiration
H	0015977	biological_process	carbon fixation
H	0015979	biological_process	photosynthesis
H	0016491	molecular_function	oxidoreductase activity
H	0016829	molecular_function	lyase activity
H	0016984	molecular_function	ribulose-bisphosphate carboxylase activity
H	0019253	biological_process	reductive pentose-phosphate cycle
H	0031469	cellular_component	bacterial microcompartment
H	0031470	cellular_component	carboxysome
H	0046872	molecular_function	metal ion binding

Functional Information from PROSITE/UniProt

site_id	PS00012
Number of Residues	16
Details	PHOSPHOPANTETHEINE Phosphopantetheine attachment site. LTGISSIEQNRLIVGA

Chain	Residue	Details
I	LEU61-ALA76

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

Chain	Residue	Details
A	GLY193-GLU201

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	16
Details	Active site: {"description":"Proton acceptor"}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	8
Details	Binding site: {"description":"in homodimeric partner"}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	38
Details	Binding site: {}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	8
Details	Binding site: {"description":"via carbamate group","evidences":[{"source":"PubMed","id":"8245022","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	16
Details	Binding site: {"evidences":[{"source":"PubMed","id":"8245022","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	8
Details	Modified residue: {"description":"N6-carboxylysine","evidences":[{"source":"PubMed","id":"16593333","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	189
Details	Region: {"description":"N-terminal alpha-helix","evidences":[{"source":"PubMed","id":"26237510","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	584
Details	Region: {"description":"C-terminal beta sheet","evidences":[{"source":"PubMed","id":"26237510","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	5
Details	M-CSA 907

Chain	Residue	Details
A	LYS172	electrostatic stabiliser, metal ligand, proton donor
A	LYS198	metal ligand, nucleophile, proton donor
A	ASP200	metal ligand
A	GLU201	metal ligand
A	HIS291	proton acceptor

site_id	MCSA2
Number of Residues	5
Details	M-CSA 907

Chain	Residue	Details
B	LYS172	electrostatic stabiliser, metal ligand, proton donor
B	LYS198	metal ligand, nucleophile, proton donor
B	ASP200	metal ligand
B	GLU201	metal ligand
B	HIS291	proton acceptor

site_id	MCSA3
Number of Residues	5
Details	M-CSA 907

Chain	Residue	Details
C	LYS172	electrostatic stabiliser, metal ligand, proton donor
C	LYS198	metal ligand, nucleophile, proton donor
C	ASP200	metal ligand
C	GLU201	metal ligand
C	HIS291	proton acceptor

site_id	MCSA4
Number of Residues	5
Details	M-CSA 907

Chain	Residue	Details
D	LYS172	electrostatic stabiliser, metal ligand, proton donor
D	LYS198	metal ligand, nucleophile, proton donor
D	ASP200	metal ligand
D	GLU201	metal ligand
D	HIS291	proton acceptor

site_id	MCSA5
Number of Residues	5
Details	M-CSA 907

Chain	Residue	Details
E	LYS172	electrostatic stabiliser, metal ligand, proton donor
E	LYS198	metal ligand, nucleophile, proton donor
E	ASP200	metal ligand
E	GLU201	metal ligand
E	HIS291	proton acceptor

site_id	MCSA6
Number of Residues	5
Details	M-CSA 907

Chain	Residue	Details
F	LYS172	electrostatic stabiliser, metal ligand, proton donor
F	LYS198	metal ligand, nucleophile, proton donor
F	ASP200	metal ligand
F	GLU201	metal ligand
F	HIS291	proton acceptor

site_id	MCSA7
Number of Residues	5
Details	M-CSA 907

Chain	Residue	Details
G	LYS172	electrostatic stabiliser, metal ligand, proton donor
G	LYS198	metal ligand, nucleophile, proton donor
G	ASP200	metal ligand
G	GLU201	metal ligand
G	HIS291	proton acceptor

site_id	MCSA8
Number of Residues	5
Details	M-CSA 907

Chain	Residue	Details
H	LYS172	electrostatic stabiliser, metal ligand, proton donor
H	LYS198	metal ligand, nucleophile, proton donor
H	ASP200	metal ligand
H	GLU201	metal ligand
H	HIS291	proton acceptor

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)