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1RBA

SUBSTITUTION OF ASP193 TO ASN AT THE ACTIVE SITE OF RIBULOSE-1,5-BISPHOSPHATE CARBOXYLASE RESULTS IN CONFORMATIONAL CHANGES

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 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
AASN193
AGLU194
BASN193
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
Detailsa catalytic site defined by CSA, PubMed 3129424, 2991249, 6778504, 8909282, 8648644, 2545684, 3151016, 1761567, 6784749, 11848907
ChainResidueDetails
AASN192
AHIS287
ALYS166
ALYS191
AHIS321

site_idCSA2
Number of Residues5
Detailsa catalytic site defined by CSA, PubMed 3129424, 2991249, 6778504, 8909282, 8648644, 2545684, 3151016, 1761567, 6784749, 11848907
ChainResidueDetails
BASN192
BHIS287
BLYS166
BLYS191
BHIS321

site_idMCSA1
Number of Residues8
DetailsM-CSA 797
ChainResidueDetails
ALYS166electrostatic stabiliser, proton acceptor, proton donor
ALYS191electron pair donor, metal ligand, nucleophile
AASN192electrostatic stabiliser
AASN193metal 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
BASN193metal ligand
BGLU194metal ligand
BHIS287activator, increase nucleophilicity, proton acceptor
BHIS321electrostatic stabiliser
BLYS329electrostatic stabiliser

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PDB entries from 2024-11-06

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