Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

4LF2

Hexameric Form II RuBisCO from Rhodopseudomonas palustris, activated and complexed with sulfate and magnesium

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0004497molecular_functionmonooxygenase activity
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
B0000287molecular_functionmagnesium ion binding
B0004497molecular_functionmonooxygenase activity
B0015977biological_processcarbon fixation
B0015979biological_processphotosynthesis
B0016491molecular_functionoxidoreductase activity
B0016829molecular_functionlyase activity
B0016984molecular_functionribulose-bisphosphate carboxylase activity
B0019253biological_processreductive pentose-phosphate cycle
B0046872molecular_functionmetal ion binding
C0000287molecular_functionmagnesium ion binding
C0004497molecular_functionmonooxygenase activity
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
D0000287molecular_functionmagnesium ion binding
D0004497molecular_functionmonooxygenase activity
D0015977biological_processcarbon fixation
D0015979biological_processphotosynthesis
D0016491molecular_functionoxidoreductase activity
D0016829molecular_functionlyase activity
D0016984molecular_functionribulose-bisphosphate carboxylase activity
D0019253biological_processreductive pentose-phosphate cycle
D0046872molecular_functionmetal ion binding
E0000287molecular_functionmagnesium ion binding
E0004497molecular_functionmonooxygenase activity
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
F0000287molecular_functionmagnesium ion binding
F0004497molecular_functionmonooxygenase activity
F0015977biological_processcarbon fixation
F0015979biological_processphotosynthesis
F0016491molecular_functionoxidoreductase activity
F0016829molecular_functionlyase activity
F0016984molecular_functionribulose-bisphosphate carboxylase activity
F0019253biological_processreductive pentose-phosphate cycle
F0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 601
ChainResidue
ALYS167
AKCX192
AASP194
AGLU195
BASN112
BHOH828

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 A 602
ChainResidue
ASER369
AHOH701
AHOH702
AHOH911
BHOH847
AARG289
AHIS322
AMET331

site_idAC3
Number of Residues9
DetailsBINDING SITE FOR RESIDUE SO4 A 603
ChainResidue
AILE165
ALYS167
ALYS330
AGLY371
AGLY394
AGLY395
AHOH788
AHOH813
BTHR54

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CO3 A 604
ChainResidue
AGLU346
AHIS386
AASN388

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MG B 601
ChainResidue
AASN112
AHOH938
AHOH939
BLYS167
BKCX192
BASP194
BGLU195

site_idAC6
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 B 602
ChainResidue
AHOH827
BARG289
BHIS322
BGLY324
BSER369
BHOH701
BHOH702
BHOH857

site_idAC7
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 B 603
ChainResidue
ATHR54
BILE165
BLYS167
BLYS330
BGLY371
BGLY394
BGLY395
BHOH863

site_idAC8
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CO3 B 604
ChainResidue
BGLU346
BASN388
BHOH805

site_idAC9
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MG C 601
ChainResidue
CLYS167
CLYS169
CKCX192
CASP194
CGLU195
DASN112
DHOH945

site_idBC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 C 602
ChainResidue
CARG289
CHIS322
CSER369
CHOH701
CHOH702
CHOH935

site_idBC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 C 603
ChainResidue
CLYS167
CLYS330
CGLY370
CGLY371
CGLY394
CGLY395
DTHR54
DASN55

site_idBC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CO3 C 604
ChainResidue
CGLU346
CASN388
CHOH927

site_idBC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG D 601
ChainResidue
CASN112
CHOH953
DKCX192
DASP194
DGLU195
DHOH944

site_idBC5
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 D 602
ChainResidue
CHOH869
DARG289
DHIS322
DSER369
DHOH701
DHOH702
DHOH776
DHOH777

site_idBC6
Number of Residues9
DetailsBINDING SITE FOR RESIDUE SO4 D 603
ChainResidue
CTHR54
DILE165
DLYS167
DLYS330
DGLY370
DGLY371
DGLY394
DGLY395
DHOH944

site_idBC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 E 701
ChainResidue
EARG289
EHIS292
EHIS322
EMET331
EHOH801
EHOH940

site_idBC8
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 E 702
ChainResidue
ELYS167
ELYS330
EGLY370
EGLY371
EGLY394
EGLY395
EHOH981
FTHR54

site_idBC9
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 F 701
ChainResidue
EHOH997
FARG289
FHIS292
FHIS322
FMET331
FHOH874
FHOH904
FHOH940

site_idCC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 F 702
ChainResidue
ETHR54
EASN55
FLYS167
FLYS330
FGLY371
FGLY394
FGLY395
FHOH980

Functional Information from PROSITE/UniProt
site_idPS00157
Number of Residues9
DetailsRUBISCO_LARGE Ribulose bisphosphate carboxylase large chain active site. GgDFiKnDE
ChainResidueDetails
AGLY187-GLU195

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues12
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_01339","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues6
DetailsBinding site: {"description":"in homodimeric partner","evidences":[{"source":"HAMAP-Rule","id":"MF_01339","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues36
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01339","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues6
DetailsBinding site: {"description":"via carbamate group","evidences":[{"source":"HAMAP-Rule","id":"MF_01339","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues6
DetailsSite: {"description":"Transition state stabilizer","evidences":[{"source":"HAMAP-Rule","id":"MF_01339","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues6
DetailsModified residue: {"description":"N6-carboxylysine","evidences":[{"source":"HAMAP-Rule","id":"MF_01339","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

244693

PDB entries from 2025-11-12

PDB statisticsPDBj update infoContact PDBjnumon