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5HQM

Structure function studies of R. palustris RubisCO (R. palustris/R. rubrum chimera)

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
Functional Information from PDB Data
site_idAC1
Number of Residues28
Detailsbinding site for residue CAP A 501
ChainResidue
AILE165
ALYS330
AMET331
ASER369
AGLY370
AGLY371
AGLY394
AGLY395
AMG502
AHOH614
AHOH617
ALYS167
AHOH644
AHOH666
AHOH681
AHOH687
AHOH688
BGLU49
BTHR54
BASN112
BHOH626
ALYS169
AKCX192
AASP194
AGLU195
AHIS288
AARG289
AHIS322

site_idAC2
Number of Residues6
Detailsbinding site for residue MG A 502
ChainResidue
ALYS169
AKCX192
AASP194
AGLU195
ACAP501
BASN112

site_idAC3
Number of Residues3
Detailsbinding site for residue K A 503
ChainResidue
ALEU10
ALEU12
ATYR73

site_idAC4
Number of Residues23
Detailsbinding site for residue CAP B 501
ChainResidue
ATHR54
AASN112
BILE165
BLYS167
BLYS169
BKCX192
BASP194
BGLU195
BHIS288
BARG289
BHIS322
BLYS330
BMET331
BSER369
BGLY370
BGLY371
BGLY394
BGLY395
BMG502
BHOH604
BHOH615
BHOH623
BHOH697

site_idAC5
Number of Residues5
Detailsbinding site for residue MG B 502
ChainResidue
AASN112
BKCX192
BASP194
BGLU195
BCAP501

site_idAC6
Number of Residues4
Detailsbinding site for residue K B 503
ChainResidue
BLEU10
BLEU12
BTYR73
BHOH718

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 Residues4
DetailsACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_01339
ChainResidueDetails
ALYS167
AHIS288
BLYS167
BHIS288

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: in homodimeric partner => ECO:0000255|HAMAP-Rule:MF_01339
ChainResidueDetails
AASN112
BASN112

site_idSWS_FT_FI3
Number of Residues12
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01339
ChainResidueDetails
AHIS322
ASER369
BLYS169
BASP194
BGLU195
BARG289
BHIS322
BSER369
ALYS169
AASP194
AGLU195
AARG289

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: via carbamate group => ECO:0000255|HAMAP-Rule:MF_01339
ChainResidueDetails
AKCX192
BKCX192

site_idSWS_FT_FI5
Number of Residues2
DetailsSITE: Transition state stabilizer => ECO:0000255|HAMAP-Rule:MF_01339
ChainResidueDetails
ALYS330
BLYS330

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: N6-carboxylysine => ECO:0000255|HAMAP-Rule:MF_01339
ChainResidueDetails
AKCX192
BKCX192

Catalytic Information from CSA
site_idMCSA1
Number of Residues
DetailsM-CSA 797
ChainResidueDetails

site_idMCSA2
Number of Residues
DetailsM-CSA 797
ChainResidueDetails

221051

PDB entries from 2024-06-12

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