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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

8RUC

ACTIVATED SPINACH RUBISCO COMPLEXED WITH 2-CARBOXYARABINITOL BISPHOSPHATE

Replaces:  8RUB
Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0004497molecular_functionmonooxygenase activity
A0009507cellular_componentchloroplast
A0009853biological_processphotorespiration
A0015977biological_processcarbon fixation
A0015979biological_processphotosynthesis
A0016491molecular_functionoxidoreductase activity
A0016829molecular_functionlyase activity
A0016984molecular_functionribulose-bisphosphate carboxylase activity
A0019253biological_processreductive pentose-phosphate cycle
A0046872molecular_functionmetal ion binding
C0000287molecular_functionmagnesium ion binding
C0004497molecular_functionmonooxygenase activity
C0009507cellular_componentchloroplast
C0009853biological_processphotorespiration
C0015977biological_processcarbon fixation
C0015979biological_processphotosynthesis
C0016491molecular_functionoxidoreductase activity
C0016829molecular_functionlyase activity
C0016984molecular_functionribulose-bisphosphate carboxylase activity
C0019253biological_processreductive pentose-phosphate cycle
C0046872molecular_functionmetal ion binding
E0000287molecular_functionmagnesium ion binding
E0004497molecular_functionmonooxygenase activity
E0009507cellular_componentchloroplast
E0009853biological_processphotorespiration
E0015977biological_processcarbon fixation
E0015979biological_processphotosynthesis
E0016491molecular_functionoxidoreductase activity
E0016829molecular_functionlyase activity
E0016984molecular_functionribulose-bisphosphate carboxylase activity
E0019253biological_processreductive pentose-phosphate cycle
E0046872molecular_functionmetal ion binding
G0000287molecular_functionmagnesium ion binding
G0004497molecular_functionmonooxygenase activity
G0009507cellular_componentchloroplast
G0009853biological_processphotorespiration
G0015977biological_processcarbon fixation
G0015979biological_processphotosynthesis
G0016491molecular_functionoxidoreductase activity
G0016829molecular_functionlyase activity
G0016984molecular_functionribulose-bisphosphate carboxylase activity
G0019253biological_processreductive pentose-phosphate cycle
G0046872molecular_functionmetal ion binding
I0009507cellular_componentchloroplast
I0009853biological_processphotorespiration
I0015977biological_processcarbon fixation
I0015979biological_processphotosynthesis
I0016984molecular_functionribulose-bisphosphate carboxylase activity
I0019253biological_processreductive pentose-phosphate cycle
J0009507cellular_componentchloroplast
J0009853biological_processphotorespiration
J0015977biological_processcarbon fixation
J0015979biological_processphotosynthesis
J0016984molecular_functionribulose-bisphosphate carboxylase activity
J0019253biological_processreductive pentose-phosphate cycle
K0009507cellular_componentchloroplast
K0009853biological_processphotorespiration
K0015977biological_processcarbon fixation
K0015979biological_processphotosynthesis
K0016984molecular_functionribulose-bisphosphate carboxylase activity
K0019253biological_processreductive pentose-phosphate cycle
L0009507cellular_componentchloroplast
L0009853biological_processphotorespiration
L0015977biological_processcarbon fixation
L0015979biological_processphotosynthesis
L0016984molecular_functionribulose-bisphosphate carboxylase activity
L0019253biological_processreductive pentose-phosphate cycle
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG A 476
ChainResidue
AKCX201
AASP203
AGLU204
ACAP477
site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG C 476
ChainResidue
CKCX201
CASP203
CGLU204
CCAP477
site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG E 476
ChainResidue
EKCX201
EASP203
EGLU204
ECAP477
site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG G 476
ChainResidue
GKCX201
GASP203
GGLU204
GCAP477
site_idAC5
Number of Residues29
DetailsBINDING SITE FOR RESIDUE CAP A 477
ChainResidue
ATHR173
ALYS175
ALYS177
AKCX201
AASP203
AGLU204
AHIS294
AARG295
AHIS327
ALYS334
ALEU335
ASER379
AGLY380
AGLY381
AGLY403
AGLY404
AMG476
AHOH483
AHOH511
AHOH621
AHOH625
AHOH673
AHOH739
AHOH748
EGLU60
ETHR65
ETRP66
EASN123
EHOH612
site_idAC6
Number of Residues29
DetailsBINDING SITE FOR RESIDUE CAP C 477
ChainResidue
CGLU60
CTHR65
CTRP66
CASN123
CTHR173
CLYS175
CLYS177
CKCX201
CASP203
CGLU204
CHIS294
CARG295
CHIS327
CLYS334
CLEU335
CSER379
CGLY380
CGLY381
CGLY403
CGLY404
CMG476
CHOH495
CHOH505
CHOH546
CHOH663
CHOH664
CHOH722
CHOH723
CHOH752
site_idAC7
Number of Residues28
DetailsBINDING SITE FOR RESIDUE CAP E 477
ChainResidue
EGLU204
EHIS294
EARG295
EHIS327
ELYS334
ELEU335
ESER379
EGLY380
EGLY381
EGLY403
EGLY404
EMG476
EHOH479
EHOH492
EHOH502
EHOH662
EHOH666
EHOH668
EHOH722
AGLU60
ATHR65
ATRP66
AASN123
ETHR173
ELYS175
ELYS177
EKCX201
EASP203
site_idAC8
Number of Residues30
DetailsBINDING SITE FOR RESIDUE CAP G 477
ChainResidue
GGLU60
GTHR65
GTRP66
GASN123
GTHR173
GLYS175
GLYS177
GKCX201
GASP203
GGLU204
GHIS294
GARG295
GHIS327
GLYS334
GLEU335
GSER379
GGLY380
GGLY381
GGLY403
GGLY404
GMG476
GHOH480
GHOH495
GHOH617
GHOH682
GHOH683
GHOH692
GHOH712
GHOH729
GHOH732
site_idACA
Number of Residues4
DetailsCATALYTIC RESIDUES
ChainResidue
AKCX201
AASP203
AGLU204
AMG476
site_idACC
Number of Residues4
DetailsCATALYTIC RESIDUES
ChainResidue
CKCX201
CASP203
CGLU204
CMG476
site_idACE
Number of Residues4
DetailsCATALYTIC RESIDUES
ChainResidue
EASP203
EGLU204
EMG476
EKCX201
site_idACG
Number of Residues4
DetailsCATALYTIC RESIDUES
ChainResidue
GKCX201
GASP203
GGLU204
GMG476
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 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":"Not N6-methylated","evidences":[{"source":"PubMed","id":"2928307","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues4
DetailsSite: {"description":"Transition state stabilizer","evidences":[{"source":"PubMed","id":"8955130","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI12
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
site_idSWS_FT_FI13
Number of Residues4
DetailsModified residue: {"description":"Methionine derivative"}
ChainResidueDetails
Catalytic Information from CSA
site_idCSA1
Number of Residues5
DetailsAnnotated By Reference To The Literature 1rbl
ChainResidueDetails
ALYS175
AHIS294
ALYS177
AASP203
AHIS327
site_idCSA2
Number of Residues5
DetailsAnnotated By Reference To The Literature 1rbl
ChainResidueDetails
CLYS175
CHIS294
CLYS177
CASP203
CHIS327
site_idCSA3
Number of Residues5
DetailsAnnotated By Reference To The Literature 1rbl
ChainResidueDetails
ELYS175
EHIS294
ELYS177
EASP203
EHIS327
site_idCSA4
Number of Residues5
DetailsAnnotated By Reference To The Literature 1rbl
ChainResidueDetails
GLYS175
GHIS294
GLYS177
GASP203
GHIS327

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PDB entries from 2025-12-10

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