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3RUB

CRYSTAL STRUCTURE OF THE UNACTIVATED FORM OF RIBULOSE-1,5-BISPHOSPHATE CARBOXYLASE(SLASH)OXYGENASE FROM TOBACCO REFINED AT 2.0-ANGSTROMS RESOLUTION

Functional Information from GO Data
ChainGOidnamespacecontents
L0000287molecular_functionmagnesium ion binding
L0004497molecular_functionmonooxygenase activity
L0005515molecular_functionprotein binding
L0009507cellular_componentchloroplast
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
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 L 490
ChainResidue
LGLY380
LGLY381
LGLY403
LGLY404
LHOH608
LHOH668

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 L 491
ChainResidue
LARG295
LHIS298
LGLY329
LHOH636

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 L 492
ChainResidue
LARG134
LLYS305
LHIS310
LILE341
LHOH578

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ASN L 493
ChainResidue
LLYS463
LGLU464
LPHE467

site_idCAT
Number of Residues13
DetailsCATALYTIC RESIDUES
ChainResidue
LLYS175
LSER379
LSO4490
LSO4491
LSO4492
LLYS177
LLYS201
LASP203
LGLU204
LHIS294
LARG295
LHIS298
LHIS327

Functional Information from PROSITE/UniProt
site_idPS00018
Number of Residues13
DetailsEF_HAND_1 EF-hand calcium-binding domain. DLSQEQLLSevEY
ChainResidueDetails
SASP20-TYR32

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 Residues2
DetailsActive site: {"description":"Proton acceptor"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsBinding site: {"description":"in homodimeric partner"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues7
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsBinding site: {"description":"via carbamate group"}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsSite: {"description":"Transition state stabilizer"}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues1
DetailsModified residue: {"description":"N6-carboxylysine","evidences":[{"source":"PubMed","id":"10801357","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues6
DetailsAnnotated By Reference To The Literature 1rbl
ChainResidueDetails
LLYS175
LLYS201
LLYS177
LHIS294
LASP203
LHIS327

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PDB entries from 2025-12-24

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