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9CI2

Anthoceros agrestis Rubisco octamer core complexed with small subunits and Arabidopsis thaliana BSD2

Functional Information from GO Data
ChainGOidnamespacecontents
10005515molecular_functionprotein binding
10005829cellular_componentcytosol
10006457biological_processprotein folding
10009507cellular_componentchloroplast
10009570cellular_componentchloroplast stroma
10044183molecular_functionprotein folding chaperone
10101031cellular_componentprotein folding chaperone complex
10110102biological_processribulose bisphosphate carboxylase complex assembly
20005515molecular_functionprotein binding
20005829cellular_componentcytosol
20006457biological_processprotein folding
20009507cellular_componentchloroplast
20009570cellular_componentchloroplast stroma
20044183molecular_functionprotein folding chaperone
20101031cellular_componentprotein folding chaperone complex
20110102biological_processribulose bisphosphate carboxylase complex assembly
30005515molecular_functionprotein binding
30005829cellular_componentcytosol
30006457biological_processprotein folding
30009507cellular_componentchloroplast
30009570cellular_componentchloroplast stroma
30044183molecular_functionprotein folding chaperone
30101031cellular_componentprotein folding chaperone complex
30110102biological_processribulose bisphosphate carboxylase complex assembly
40005515molecular_functionprotein binding
40005829cellular_componentcytosol
40006457biological_processprotein folding
40009507cellular_componentchloroplast
40009570cellular_componentchloroplast stroma
40044183molecular_functionprotein folding chaperone
40101031cellular_componentprotein folding chaperone complex
40110102biological_processribulose bisphosphate carboxylase complex assembly
A0000287molecular_functionmagnesium ion binding
A0009507cellular_componentchloroplast
A0015977biological_processcarbon fixation
A0016984molecular_functionribulose-bisphosphate carboxylase activity
A0019253biological_processreductive pentose-phosphate cycle
B0000287molecular_functionmagnesium ion binding
B0009507cellular_componentchloroplast
B0015977biological_processcarbon fixation
B0016984molecular_functionribulose-bisphosphate carboxylase activity
B0019253biological_processreductive pentose-phosphate cycle
C0000287molecular_functionmagnesium ion binding
C0009507cellular_componentchloroplast
C0015977biological_processcarbon fixation
C0016984molecular_functionribulose-bisphosphate carboxylase activity
C0019253biological_processreductive pentose-phosphate cycle
D0000287molecular_functionmagnesium ion binding
D0009507cellular_componentchloroplast
D0015977biological_processcarbon fixation
D0016984molecular_functionribulose-bisphosphate carboxylase activity
D0019253biological_processreductive pentose-phosphate cycle
E0000287molecular_functionmagnesium ion binding
E0009507cellular_componentchloroplast
E0015977biological_processcarbon fixation
E0016984molecular_functionribulose-bisphosphate carboxylase activity
E0019253biological_processreductive pentose-phosphate cycle
F0000287molecular_functionmagnesium ion binding
F0009507cellular_componentchloroplast
F0015977biological_processcarbon fixation
F0016984molecular_functionribulose-bisphosphate carboxylase activity
F0019253biological_processreductive pentose-phosphate cycle
G0000287molecular_functionmagnesium ion binding
G0009507cellular_componentchloroplast
G0015977biological_processcarbon fixation
G0016984molecular_functionribulose-bisphosphate carboxylase activity
G0019253biological_processreductive pentose-phosphate cycle
H0000287molecular_functionmagnesium ion binding
H0009507cellular_componentchloroplast
H0015977biological_processcarbon fixation
H0016984molecular_functionribulose-bisphosphate carboxylase activity
H0019253biological_processreductive pentose-phosphate cycle
Functional Information from PROSITE/UniProt
site_idPS00157
Number of Residues9
DetailsRUBISCO_LARGE Ribulose bisphosphate carboxylase large chain active site. GlDFtKdDE
ChainResidueDetails
AGLY196-GLU204

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues32
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"29217567","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6EKB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6EKC","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues12
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"29217567","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6EKB","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues16
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_01338","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues8
DetailsBinding site: {"description":"in homodimeric partner","evidences":[{"source":"HAMAP-Rule","id":"MF_01338","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues56
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01338","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues8
DetailsBinding site: {"description":"via carbamate group","evidences":[{"source":"HAMAP-Rule","id":"MF_01338","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues8
DetailsSite: {"description":"Transition state stabilizer","evidences":[{"source":"HAMAP-Rule","id":"MF_01338","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues8
DetailsModified residue: {"description":"N6-carboxylysine","evidences":[{"source":"HAMAP-Rule","id":"MF_01338","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues4
DetailsModified residue: {"description":"N6,N6,N6-trimethyllysine","evidences":[{"source":"HAMAP-Rule","id":"MF_01338","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

254227

PDB entries from 2026-05-27

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