Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

1RUS

CRYSTAL STRUCTURE OF THE BINARY COMPLEX OF RIBULOSE-1,5-BISPHOSPHATE CARBOXYLASE AND ITS PRODUCT, 3-PHOSPHO-D-GLYCERATE

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 Residues8
DetailsBINDING SITE FOR RESIDUE 3PG A 500
ChainResidue
AILE164
AHIS287
AARG288
AHIS321
ATHR322
AGLY323
ASER368
BASN111

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE 3PG B 500
ChainResidue
BHIS287
BARG288
BHIS321
BGLY323
AASN111

Functional Information from PROSITE/UniProt
site_idPS00157
Number of Residues9
DetailsRUBISCO_LARGE Ribulose bisphosphate carboxylase large chain active site. GgDFiKnDE
ChainResidueDetails
AGLY186-GLU194

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: Proton acceptor
ChainResidueDetails
ALYS166
AHIS287
BLYS166
BHIS287

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: in homodimeric partner
ChainResidueDetails
AASN111
BASN111

site_idSWS_FT_FI3
Number of Residues8
DetailsBINDING:
ChainResidueDetails
ALYS168
AARG288
AHIS321
ASER368
BLYS168
BARG288
BHIS321
BSER368

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: via carbamate group => ECO:0000269|PubMed:1899197, ECO:0000269|Ref.4
ChainResidueDetails
ALYS191
BLYS191

site_idSWS_FT_FI5
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:1899197, ECO:0000269|Ref.4
ChainResidueDetails
AASP193
AGLU194
BASP193
BGLU194

site_idSWS_FT_FI6
Number of Residues2
DetailsSITE: Transition state stabilizer
ChainResidueDetails
ALYS329
BLYS329

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: N6-carboxylysine => ECO:0000269|PubMed:1899197
ChainResidueDetails
ALYS191
BLYS191

Catalytic Information from CSA
site_idCSA1
Number of Residues5
DetailsAnnotated By Reference To The Literature 1rbl
ChainResidueDetails
AASN192
AHIS287
ALYS166
ALYS191
AHIS321

site_idCSA2
Number of Residues5
DetailsAnnotated By Reference To The Literature 1rbl
ChainResidueDetails
BASN192
BHIS287
BLYS166
BLYS191
BHIS321

site_idCSA3
Number of Residues6
DetailsAnnotated By Reference To The Literature 1rbl
ChainResidueDetails
AHIS287
ALYS166
AASP193
ALYS191
AHIS321
ALYS168

site_idCSA4
Number of Residues6
DetailsAnnotated By Reference To The Literature 1rbl
ChainResidueDetails
BHIS287
BLYS166
BASP193
BLYS191
BHIS321
BLYS168

site_idMCSA1
Number of Residues8
DetailsM-CSA 797
ChainResidueDetails
ALYS166electrostatic stabiliser, proton acceptor, proton donor
ALYS191electron pair donor, metal ligand, nucleophile
AASN192electrostatic stabiliser
AASP193metal ligand
AGLU194metal ligand
AHIS287activator, increase nucleophilicity, proton acceptor
AHIS321electrostatic stabiliser
ALYS329electrostatic stabiliser

site_idMCSA2
Number of Residues8
DetailsM-CSA 797
ChainResidueDetails
BLYS166electrostatic stabiliser, proton acceptor, proton donor
BLYS191electron pair donor, metal ligand, nucleophile
BASN192electrostatic stabiliser
BASP193metal ligand
BGLU194metal ligand
BHIS287activator, increase nucleophilicity, proton acceptor
BHIS321electrostatic stabiliser
BLYS329electrostatic stabiliser

227111

PDB entries from 2024-11-06

PDB statisticsPDBj update infoContact PDBjnumon