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5HJY

Structure function studies of R. palustris RubisCO (I165T mutant; CABP-bound)

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0015977biological_processcarbon fixation
A0016984molecular_functionribulose-bisphosphate carboxylase activity
B0000287molecular_functionmagnesium ion binding
B0015977biological_processcarbon fixation
B0016984molecular_functionribulose-bisphosphate carboxylase activity
C0000287molecular_functionmagnesium ion binding
C0015977biological_processcarbon fixation
C0016984molecular_functionribulose-bisphosphate carboxylase activity
D0000287molecular_functionmagnesium ion binding
D0015977biological_processcarbon fixation
D0016984molecular_functionribulose-bisphosphate carboxylase activity
E0000287molecular_functionmagnesium ion binding
E0015977biological_processcarbon fixation
E0016984molecular_functionribulose-bisphosphate carboxylase activity
F0000287molecular_functionmagnesium ion binding
F0015977biological_processcarbon fixation
F0016984molecular_functionribulose-bisphosphate carboxylase activity
Functional Information from PDB Data
site_idAC1
Number of Residues29
Detailsbinding site for residue CAP A 500
ChainResidue
ATHR165
ALYS330
AMET331
ASER369
AGLY370
AGLY371
AGLY394
AGLY395
AMG501
AHOH617
AHOH623
ALYS167
AHOH628
AHOH653
AHOH656
AHOH662
AHOH668
AHOH675
AHOH682
BGLU49
BTHR54
BASN112
ALYS169
AKCX192
AASP194
AGLU195
AHIS288
AARG289
AHIS322

site_idAC2
Number of Residues6
Detailsbinding site for residue MG A 501
ChainResidue
ALYS169
AKCX192
AASP194
AGLU195
ACAP500
BASN112

site_idAC3
Number of Residues27
Detailsbinding site for residue CAP B 500
ChainResidue
AGLU49
ATHR54
AASN112
AHOH605
AHOH711
BTHR165
BLYS167
BLYS169
BKCX192
BASP194
BGLU195
BHIS288
BARG289
BHIS322
BLYS330
BSER369
BGLY370
BGLY371
BALA393
BGLY394
BGLY395
BMG501
BHOH612
BHOH613
BHOH649
BHOH672
BHOH714

site_idAC4
Number of Residues6
Detailsbinding site for residue MG B 501
ChainResidue
AASN112
BLYS169
BKCX192
BASP194
BGLU195
BCAP500

site_idAC5
Number of Residues30
Detailsbinding site for residue CAP C 500
ChainResidue
CTHR165
CLYS167
CLYS169
CKCX192
CASP194
CGLU195
CHIS288
CARG289
CHIS322
CLYS330
CMET331
CSER369
CGLY370
CGLY371
CGLY394
CGLY395
CMG501
CHOH610
CHOH611
CHOH622
CHOH626
CHOH662
CHOH676
CHOH681
CHOH684
CHOH748
DGLU49
DTHR54
DASN112
DHOH637

site_idAC6
Number of Residues6
Detailsbinding site for residue MG C 501
ChainResidue
CKCX192
CASP194
CGLU195
CCAP500
DASN112
CLYS169

site_idAC7
Number of Residues30
Detailsbinding site for residue CAP D 501
ChainResidue
CGLU49
CTHR54
CASN112
CHOH658
CHOH679
DTHR165
DLYS167
DLYS169
DKCX192
DASP194
DGLU195
DHIS288
DARG289
DHIS322
DLYS330
DMET331
DSER369
DGLY370
DGLY371
DGLY394
DGLY395
DMG502
DHOH607
DHOH613
DHOH634
DHOH653
DHOH663
DHOH697
DHOH749
DHOH758

site_idAC8
Number of Residues6
Detailsbinding site for residue MG D 502
ChainResidue
CASN112
DLYS169
DKCX192
DASP194
DGLU195
DCAP501

site_idAC9
Number of Residues2
Detailsbinding site for residue CL D 503
ChainResidue
DARG22
DARG93

site_idAD1
Number of Residues29
Detailsbinding site for residue CAP E 500
ChainResidue
ETHR165
ELYS167
ELYS169
EKCX192
EASP194
EGLU195
EHIS288
EARG289
EHIS322
ELYS330
EMET331
ESER369
EGLY370
EGLY371
EGLY394
EGLY395
EMG501
EHOH605
EHOH609
EHOH626
EHOH640
EHOH694
EHOH697
FGLU49
FTHR54
FASN112
FHOH668
FHOH673
FHOH702

site_idAD2
Number of Residues6
Detailsbinding site for residue MG E 501
ChainResidue
ELYS169
EKCX192
EASP194
EGLU195
ECAP500
FASN112

site_idAD3
Number of Residues29
Detailsbinding site for residue CAP F 500
ChainResidue
EGLU49
ETHR54
EASN112
EHOH718
FTHR165
FLYS167
FLYS169
FKCX192
FASP194
FGLU195
FHIS288
FARG289
FHIS322
FLYS330
FSER369
FGLY370
FGLY371
FALA393
FGLY394
FGLY395
FMG501
FHOH602
FHOH610
FHOH639
FHOH641
FHOH643
FHOH649
FHOH692
FHOH694

site_idAD4
Number of Residues6
Detailsbinding site for residue MG F 501
ChainResidue
EASN112
FLYS169
FKCX192
FASP194
FGLU195
FCAP500

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

254227

PDB entries from 2026-05-27

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