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6JX2

Crystal structure of Ketol-acid reductoisomerase from Corynebacterium glutamicum

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0004455molecular_functionketol-acid reductoisomerase activity
A0005829cellular_componentcytosol
A0008652biological_processamino acid biosynthetic process
A0008677molecular_function2-dehydropantoate 2-reductase activity
A0009082biological_processbranched-chain amino acid biosynthetic process
A0009097biological_processisoleucine biosynthetic process
A0009099biological_processL-valine biosynthetic process
A0016491molecular_functionoxidoreductase activity
A0046872molecular_functionmetal ion binding
A0050661molecular_functionNADP binding
B0000287molecular_functionmagnesium ion binding
B0004455molecular_functionketol-acid reductoisomerase activity
B0005829cellular_componentcytosol
B0008652biological_processamino acid biosynthetic process
B0008677molecular_function2-dehydropantoate 2-reductase activity
B0009082biological_processbranched-chain amino acid biosynthetic process
B0009097biological_processisoleucine biosynthetic process
B0009099biological_processL-valine biosynthetic process
B0016491molecular_functionoxidoreductase activity
B0046872molecular_functionmetal ion binding
B0050661molecular_functionNADP binding
C0000287molecular_functionmagnesium ion binding
C0004455molecular_functionketol-acid reductoisomerase activity
C0005829cellular_componentcytosol
C0008652biological_processamino acid biosynthetic process
C0008677molecular_function2-dehydropantoate 2-reductase activity
C0009082biological_processbranched-chain amino acid biosynthetic process
C0009097biological_processisoleucine biosynthetic process
C0009099biological_processL-valine biosynthetic process
C0016491molecular_functionoxidoreductase activity
C0046872molecular_functionmetal ion binding
C0050661molecular_functionNADP binding
D0000287molecular_functionmagnesium ion binding
D0004455molecular_functionketol-acid reductoisomerase activity
D0005829cellular_componentcytosol
D0008652biological_processamino acid biosynthetic process
D0008677molecular_function2-dehydropantoate 2-reductase activity
D0009082biological_processbranched-chain amino acid biosynthetic process
D0009097biological_processisoleucine biosynthetic process
D0009099biological_processL-valine biosynthetic process
D0016491molecular_functionoxidoreductase activity
D0046872molecular_functionmetal ion binding
D0050661molecular_functionNADP binding
Functional Information from PDB Data
site_idAC1
Number of Residues2
Detailsbinding site for residue MG A 401
ChainResidue
AASP192
AGLU196

site_idAC2
Number of Residues4
Detailsbinding site for residue MG A 402
ChainResidue
AGLU228
AGLU232
BASP192
BGLU196

site_idAC3
Number of Residues5
Detailsbinding site for residue MG A 403
ChainResidue
AASN100
AASP103
AALA73
AALA75
AASN98

site_idAC4
Number of Residues2
Detailsbinding site for residue MG A 404
ChainResidue
ATYR250
AASP254

site_idAC5
Number of Residues15
Detailsbinding site for residue NAP A 405
ChainResidue
AGLY25
ATYR26
AGLY27
ASER28
AARG49
ASER52
ALYS53
ASER54
ATHR68
ALEU81
AALA82
APRO83
AILE90
AHOH509
AHOH533

site_idAC6
Number of Residues2
Detailsbinding site for residue EDO A 406
ChainResidue
AGLU297
AHOH514

site_idAC7
Number of Residues4
Detailsbinding site for residue EDO A 407
ChainResidue
AASP116
AASP155
AGLN156
AHOH518

site_idAC8
Number of Residues3
Detailsbinding site for residue MG B 401
ChainResidue
AASP192
BGLU228
BGLU232

site_idAC9
Number of Residues2
Detailsbinding site for residue MG B 402
ChainResidue
BASP192
BGLU196

site_idAD1
Number of Residues1
Detailsbinding site for residue MG B 403
ChainResidue
BASP116

site_idAD2
Number of Residues1
Detailsbinding site for residue MG B 404
ChainResidue
BASP254

site_idAD3
Number of Residues4
Detailsbinding site for residue MG B 405
ChainResidue
BALA73
BALA75
BASN100
BASP103

site_idAD4
Number of Residues2
Detailsbinding site for residue EDO B 406
ChainResidue
BASP123
BGLU213

site_idAD5
Number of Residues4
Detailsbinding site for residue EDO B 407
ChainResidue
BGLU4
BLEU5
DASP10
DASN298

site_idAD6
Number of Residues3
Detailsbinding site for residue EDO B 408
ChainResidue
BHIS114
BTHR184
BGLU186

site_idAD7
Number of Residues2
Detailsbinding site for residue MG C 401
ChainResidue
CASP192
CGLU196

site_idAD8
Number of Residues3
Detailsbinding site for residue MG C 402
ChainResidue
CGLU228
CGLU232
DASP192

site_idAD9
Number of Residues19
Detailsbinding site for residue NAP C 403
ChainResidue
CGLY25
CTYR26
CGLY27
CSER28
CGLN29
CSER52
CSER54
CTHR68
CLEU81
CALA82
CPRO83
CASP84
CGLN87
CILE90
CGLY108
CHIS109
CGLY133
CPRO134
CHOH501

site_idAE1
Number of Residues4
Detailsbinding site for residue MG D 401
ChainResidue
CASP192
CGLU196
DGLU228
DGLU232

site_idAE2
Number of Residues2
Detailsbinding site for residue MG D 402
ChainResidue
DASP192
DGLU196

site_idAE3
Number of Residues12
Detailsbinding site for residue NAP D 403
ChainResidue
DGLY25
DTYR26
DGLY27
DSER28
DARG49
DSER52
DLYS53
DSER54
DTHR68
DLEU81
DPRO83
DILE90

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues720
DetailsDomain: {"description":"KARI N-terminal Rossmann","evidences":[{"source":"PROSITE-ProRule","id":"PRU01197","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues4
DetailsActive site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00435","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues60
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00435","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues145
DetailsDomain: {"description":"KARI C-terminal knotted","evidences":[{"source":"PROSITE-ProRule","id":"PRU01198","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

250359

PDB entries from 2026-03-11

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