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8EP7

Crystal Structure of the Ketol-acid Reductoisomerase from Bacillus anthracis in complex with NADP

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0004455molecular_functionketol-acid reductoisomerase activity
A0005829cellular_componentcytosol
A0008652biological_processamino acid biosynthetic process
A0009082biological_processbranched-chain amino acid biosynthetic process
A0009097biological_processisoleucine biosynthetic process
A0009099biological_processvaline 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
B0009082biological_processbranched-chain amino acid biosynthetic process
B0009097biological_processisoleucine biosynthetic process
B0009099biological_processvaline 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
C0009082biological_processbranched-chain amino acid biosynthetic process
C0009097biological_processisoleucine biosynthetic process
C0009099biological_processvaline biosynthetic process
C0016491molecular_functionoxidoreductase activity
C0046872molecular_functionmetal ion binding
C0050661molecular_functionNADP binding
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsACT_SITE: ACT_SITE => ECO:0000255|HAMAP-Rule:MF_00435
ChainResidueDetails
AHIS106
BHIS106
CHIS106

site_idSWS_FT_FI2
Number of Residues30
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00435
ChainResidueDetails
ATYR24
AARG47
ASER51
AASP81
AGLY132
AASP189
AGLU193
AGLU225
AGLU229
ASER250
BTYR24
BARG47
BSER51
BASP81
BGLY132
BASP189
BGLU193
BGLU225
BGLU229
BSER250
CTYR24
CARG47
CSER51
CASP81
CGLY132
CASP189
CGLU193
CGLU225
CGLU229
CSER250

221051

PDB entries from 2024-06-12

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