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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
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
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
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
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
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
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
DetailsACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_01339
ChainResidueDetails
ALYS167
AHIS288
BLYS167
BHIS288
CLYS167
CHIS288
DLYS167
DHIS288
ELYS167
EHIS288
FLYS167
FHIS288

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: in homodimeric partner => ECO:0000255|HAMAP-Rule:MF_01339
ChainResidueDetails
AASN112
BASN112
CASN112
DASN112
EASN112
FASN112

site_idSWS_FT_FI3
Number of Residues36
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01339
ChainResidueDetails
CLYS169
CASP194
CGLU195
CARG289
CHIS322
CSER369
DLYS169
DASP194
DGLU195
DARG289
DHIS322
DSER369
ELYS169
EASP194
EGLU195
EARG289
EHIS322
ESER369
FLYS169
FASP194
FGLU195
FARG289
FHIS322
FSER369
ALYS169
AASP194
AGLU195
AARG289
AHIS322
ASER369
BLYS169
BASP194
BGLU195
BARG289
BHIS322
BSER369

site_idSWS_FT_FI4
Number of Residues6
DetailsBINDING: via carbamate group => ECO:0000255|HAMAP-Rule:MF_01339
ChainResidueDetails
AKCX192
BKCX192
CKCX192
DKCX192
EKCX192
FKCX192

site_idSWS_FT_FI5
Number of Residues6
DetailsSITE: Transition state stabilizer => ECO:0000255|HAMAP-Rule:MF_01339
ChainResidueDetails
ALYS330
BLYS330
CLYS330
DLYS330
ELYS330
FLYS330

site_idSWS_FT_FI6
Number of Residues6
DetailsMOD_RES: N6-carboxylysine => ECO:0000255|HAMAP-Rule:MF_01339
ChainResidueDetails
AKCX192
BKCX192
CKCX192
DKCX192
EKCX192
FKCX192

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PDB entries from 2024-05-15

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