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3R8W

Structure of 3-isopropylmalate dehydrogenase isoform 2 from Arabidopsis thaliana at 2.2 angstrom resolution

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0003862molecular_function3-isopropylmalate dehydrogenase activity
A0005829cellular_componentcytosol
A0009098biological_processL-leucine biosynthetic process
A0009507cellular_componentchloroplast
A0009536cellular_componentplastid
A0009553biological_processembryo sac development
A0009555biological_processpollen development
A0009570cellular_componentchloroplast stroma
A0009941cellular_componentchloroplast envelope
A0016491molecular_functionoxidoreductase activity
A0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
A0042803molecular_functionprotein homodimerization activity
A0046872molecular_functionmetal ion binding
A0051287molecular_functionNAD binding
A0070403molecular_functionNAD+ binding
B0000287molecular_functionmagnesium ion binding
B0003862molecular_function3-isopropylmalate dehydrogenase activity
B0005829cellular_componentcytosol
B0009098biological_processL-leucine biosynthetic process
B0009507cellular_componentchloroplast
B0009536cellular_componentplastid
B0009553biological_processembryo sac development
B0009555biological_processpollen development
B0009570cellular_componentchloroplast stroma
B0009941cellular_componentchloroplast envelope
B0016491molecular_functionoxidoreductase activity
B0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
B0042803molecular_functionprotein homodimerization activity
B0046872molecular_functionmetal ion binding
B0051287molecular_functionNAD binding
B0070403molecular_functionNAD+ binding
C0000287molecular_functionmagnesium ion binding
C0003862molecular_function3-isopropylmalate dehydrogenase activity
C0005829cellular_componentcytosol
C0009098biological_processL-leucine biosynthetic process
C0009507cellular_componentchloroplast
C0009536cellular_componentplastid
C0009553biological_processembryo sac development
C0009555biological_processpollen development
C0009570cellular_componentchloroplast stroma
C0009941cellular_componentchloroplast envelope
C0016491molecular_functionoxidoreductase activity
C0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
C0042803molecular_functionprotein homodimerization activity
C0046872molecular_functionmetal ion binding
C0051287molecular_functionNAD binding
C0070403molecular_functionNAD+ binding
D0000287molecular_functionmagnesium ion binding
D0003862molecular_function3-isopropylmalate dehydrogenase activity
D0005829cellular_componentcytosol
D0009098biological_processL-leucine biosynthetic process
D0009507cellular_componentchloroplast
D0009536cellular_componentplastid
D0009553biological_processembryo sac development
D0009555biological_processpollen development
D0009570cellular_componentchloroplast stroma
D0009941cellular_componentchloroplast envelope
D0016491molecular_functionoxidoreductase activity
D0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
D0042803molecular_functionprotein homodimerization activity
D0046872molecular_functionmetal ion binding
D0051287molecular_functionNAD binding
D0070403molecular_functionNAD+ binding
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ACT A 368
ChainResidue
ALYS151
APHE161
BGLU146

site_idAC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE ACT A 369
ChainResidue
AHIS169
AARG173

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ACT A 370
ChainResidue
AGLU91
AARG98
AARG108
AARG136

site_idAC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE ACT A 371
ChainResidue
AASP235
AGLN238

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ACT A 372
ChainResidue
AILE15
AASN296
AASP337
AHOH487

site_idAC6
Number of Residues2
DetailsBINDING SITE FOR RESIDUE ACT B 368
ChainResidue
BHIS169
BARG173

site_idAC7
Number of Residues2
DetailsBINDING SITE FOR RESIDUE ACT B 369
ChainResidue
BASP235
BGLN238

site_idAC8
Number of Residues2
DetailsBINDING SITE FOR RESIDUE ACT B 370
ChainResidue
BASP254
BILE282

site_idAC9
Number of Residues2
DetailsBINDING SITE FOR RESIDUE ACT B 371
ChainResidue
BASN296
BASP337

site_idBC1
Number of Residues1
DetailsBINDING SITE FOR RESIDUE ACT B 372
ChainResidue
BARG207

site_idBC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ACT B 373
ChainResidue
BGLU91
BARG98
BARG108
BARG136

site_idBC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ACT C 368
ChainResidue
CARG98
CARG108
CARG136

site_idBC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ACT D 368
ChainResidue
DGLU91
DARG98
DARG108
DARG136

site_idBC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ACT D 369
ChainResidue
DASP235
DLYS237
DGLN238

site_idBC6
Number of Residues2
DetailsBINDING SITE FOR RESIDUE ACT D 370
ChainResidue
DARG108
DASP254

Functional Information from PROSITE/UniProt
site_idPS00470
Number of Residues20
DetailsIDH_IMDH Isocitrate and isopropylmalate dehydrogenases signature. NIFGDIlSDeaSmit.GSIGM
ChainResidueDetails
AASN246-MET265

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues16
DetailsBINDING: BINDING => ECO:0000269|PubMed:27137927, ECO:0007744|PDB:5J33
ChainResidueDetails
AILE76
AASN196
AASN227
CILE76
CASN196
CASN227
CGLU280
DILE76
DASN196
DASN227
DGLU280
AGLU280
BILE76
BASN196
BASN227
BGLU280

site_idSWS_FT_FI2
Number of Residues16
DetailsBINDING: BINDING => ECO:0000269|PubMed:27137927, ECO:0007744|PDB:5J32
ChainResidueDetails
AARG98
AARG108
AARG136
AASP226
DARG98
DARG108
DARG136
DASP226
BARG98
BARG108
BARG136
BASP226
CARG98
CARG108
CARG136
CASP226

site_idSWS_FT_FI3
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:27137927, ECO:0007744|PDB:5J32, ECO:0007744|PDB:5J33, ECO:0007744|PDB:5J34
ChainResidueDetails
AASP250
AASP254
BASP250
BASP254
CASP250
CASP254
DASP250
DASP254

site_idSWS_FT_FI4
Number of Residues4
DetailsSITE: Confers substrate specificity => ECO:0000269|PubMed:21697089
ChainResidueDetails
ALEU95
BLEU95
CLEU95
DLEU95

site_idSWS_FT_FI5
Number of Residues8
DetailsSITE: Important for catalysis => ECO:0000269|PubMed:27137927
ChainResidueDetails
CTYR143
CLYS194
DTYR143
DLYS194
ATYR143
ALYS194
BTYR143
BLYS194

site_idSWS_FT_FI6
Number of Residues8
DetailsSITE: Essential for redox regulation => ECO:0000250|UniProtKB:Q9FMT1
ChainResidueDetails
ACYS190
ACYS348
BCYS190
BCYS348
CCYS190
CCYS348
DCYS190
DCYS348

site_idSWS_FT_FI7
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q9FMT1
ChainResidueDetails
ASER32
BSER32
CSER32
DSER32

221051

PDB entries from 2024-06-12

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