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8QJ0

Room-temperature Serial Synchrotron Crystallography structure of Spinacia oleracea RuBisCO

Functional Information from GO Data
ChainGOidnamespacecontents
L0000287molecular_functionmagnesium ion binding
L0004497molecular_functionmonooxygenase activity
L0009507cellular_componentchloroplast
L0009536cellular_componentplastid
L0009853biological_processphotorespiration
L0015977biological_processcarbon fixation
L0015979biological_processphotosynthesis
L0016491molecular_functionoxidoreductase activity
L0016829molecular_functionlyase activity
L0016984molecular_functionribulose-bisphosphate carboxylase activity
L0019253biological_processreductive pentose-phosphate cycle
L0046872molecular_functionmetal ion binding
M0000287molecular_functionmagnesium ion binding
M0004497molecular_functionmonooxygenase activity
M0009507cellular_componentchloroplast
M0009536cellular_componentplastid
M0009853biological_processphotorespiration
M0015977biological_processcarbon fixation
M0015979biological_processphotosynthesis
M0016491molecular_functionoxidoreductase activity
M0016829molecular_functionlyase activity
M0016984molecular_functionribulose-bisphosphate carboxylase activity
M0019253biological_processreductive pentose-phosphate cycle
M0046872molecular_functionmetal ion binding
N0000287molecular_functionmagnesium ion binding
N0004497molecular_functionmonooxygenase activity
N0009507cellular_componentchloroplast
N0009536cellular_componentplastid
N0009853biological_processphotorespiration
N0015977biological_processcarbon fixation
N0015979biological_processphotosynthesis
N0016491molecular_functionoxidoreductase activity
N0016829molecular_functionlyase activity
N0016984molecular_functionribulose-bisphosphate carboxylase activity
N0019253biological_processreductive pentose-phosphate cycle
N0046872molecular_functionmetal ion binding
O0000287molecular_functionmagnesium ion binding
O0004497molecular_functionmonooxygenase activity
O0009507cellular_componentchloroplast
O0009536cellular_componentplastid
O0009853biological_processphotorespiration
O0015977biological_processcarbon fixation
O0015979biological_processphotosynthesis
O0016491molecular_functionoxidoreductase activity
O0016829molecular_functionlyase activity
O0016984molecular_functionribulose-bisphosphate carboxylase activity
O0019253biological_processreductive pentose-phosphate cycle
O0046872molecular_functionmetal ion binding
Functional Information from PROSITE/UniProt
site_idPS00157
Number of Residues9
DetailsRUBISCO_LARGE Ribulose bisphosphate carboxylase large chain active site. GlDFtKdDE
ChainResidueDetails
LGLY196-GLU204

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"2118958","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"637859","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9092835","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues4
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"637859","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues20
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"9034362","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1RCX","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues4
DetailsBinding site: {"description":"in homodimeric partner","evidences":[{"source":"PubMed","id":"9034362","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1RCX","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues12
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues4
DetailsBinding site: {"description":"via carbamate group","evidences":[{"source":"PubMed","id":"8648644","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9092835","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14596800","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"2118958","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"9034362","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"8648644","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9092835","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14596800","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"2118958","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"9034362","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"9034362","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1RXO","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues12
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"9034362","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1RCX","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1RXO","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues4
DetailsSite: {"description":"Transition state stabilizer","evidences":[{"source":"PubMed","id":"8955130","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues4
DetailsModified residue: {"description":"N6-carboxylysine","evidences":[{"source":"PubMed","id":"14596800","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"2118958","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8648644","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9034362","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9092835","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

239803

PDB entries from 2025-08-06

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