3RG6

Crystal structure of a chaperone-bound assembly intermediate of form I Rubisco

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	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	0031470	cellular_component	carboxysome
B	0046872	molecular_function	metal ion binding
C	0005515	molecular_function	protein binding
C	0005737	cellular_component	cytoplasm
C	0006457	biological_process	protein folding
C	0015977	biological_process	carbon fixation
C	0015979	biological_process	photosynthesis
C	0031470	cellular_component	carboxysome
C	0042803	molecular_function	protein homodimerization activity
C	0044183	molecular_function	protein folding chaperone
C	0110102	biological_process	ribulose bisphosphate carboxylase complex assembly
D	0005515	molecular_function	protein binding
D	0005737	cellular_component	cytoplasm
D	0006457	biological_process	protein folding
D	0015977	biological_process	carbon fixation
D	0015979	biological_process	photosynthesis
D	0031470	cellular_component	carboxysome
D	0042803	molecular_function	protein homodimerization activity
D	0044183	molecular_function	protein folding chaperone
D	0110102	biological_process	ribulose bisphosphate carboxylase complex assembly
E	0005515	molecular_function	protein binding
E	0005737	cellular_component	cytoplasm
E	0006457	biological_process	protein folding
E	0015977	biological_process	carbon fixation
E	0015979	biological_process	photosynthesis
E	0031470	cellular_component	carboxysome
E	0042803	molecular_function	protein homodimerization activity
E	0044183	molecular_function	protein folding chaperone
E	0110102	biological_process	ribulose bisphosphate carboxylase complex assembly
F	0005515	molecular_function	protein binding
F	0005737	cellular_component	cytoplasm
F	0006457	biological_process	protein folding
F	0015977	biological_process	carbon fixation
F	0015979	biological_process	photosynthesis
F	0031470	cellular_component	carboxysome
F	0042803	molecular_function	protein homodimerization activity
F	0044183	molecular_function	protein folding chaperone
F	0110102	biological_process	ribulose bisphosphate carboxylase complex assembly

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	GLY193-GLU201

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	12
Details	Motif: {"description":"Interacts with RbcX2","evidences":[{"source":"PubMed","id":"17574029","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	4
Details	Active site: {"description":"Proton acceptor"}

Chain

Residue

Details

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site_id	SWS_FT_FI3
Number of Residues	2
Details	Binding site: {"description":"in homodimeric partner"}

Chain

Residue

Details

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site_id	SWS_FT_FI4
Number of Residues	10
Details	Binding site: {}

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site_id	SWS_FT_FI5
Number of Residues	2
Details	Binding site: {"description":"via carbamate group","evidences":[{"source":"PubMed","id":"8245022","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI6
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"8245022","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI7
Number of Residues	2
Details	Site: {"description":"Transition state stabilizer"}

Chain

Residue

Details

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site_id	SWS_FT_FI8
Number of Residues	2
Details	Modified residue: {"description":"N6-carboxylysine","evidences":[{"source":"PubMed","id":"16593333","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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Catalytic Information from CSA

site_id	MCSA1
Number of Residues	6
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
A	LYS331	electrostatic stabiliser

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site_id	MCSA2
Number of Residues	6
Details	M-CSA 907

Chain

Residue

Details

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