Structure of PDB 4xxv Chain B

Receptor sequence
>4xxvB (length=355) Species: 271848 (Burkholderia thailandensis E264) [Search protein sequence]
MKIAVLPGDGIGPEIVNEAVKVLNALDEKFELEHAPVGGAGYEASGHPLP
DATLALAKEADAILFGAVGDWKYDSLERALRPEQAILGLRKHLELFANFR
PAICYPQLVDASPLKPELVAGLDILIVRELNGDIYFGQPRGVRAAPDGPF
AGEREGFDTMRYSEPEVRRIAHVAFQAAQKRAKKLLSVDKSNVLETSQFW
RDVMIDVSKEYADVELSHMYVDNAAMQLAKAPKQFDVIVTGNMFGDILSD
EASMLTGSIGMLPSASLDKNNKGLYEPSHGSAPDIAGKGIANPLATILSA
AMLLRYSLNRAEQADRIERAVKTVLEQGYRTGDIATPGCRQVGTAAMGDA
VVAAL
3D structure
PDB4xxv Crystal structure of 3-isopropylmalate dehydrogenase from Burkholderia thailandensis in complex with NAD
ChainB
Resolution1.7 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) Y135 K190 D222 D246 D250
Catalytic site (residue number reindexed from 1) Y135 K190 D222 D246 D250
Enzyme Commision number 1.1.1.85: 3-isopropylmalate dehydrogenase.
Interaction with ligand
Site
#
Ligand Ligand
chain
Binding residues on receptor
(original residue number in PDB)
Binding residues on receptor
(residue number reindexed from 1)
Binding affinity
BS01 NAD B I11 A67 V68 G69 E83 I259 H279 G280 S281 A282 D284 I285 A291 N292 I11 A67 V68 G69 E83 I259 H279 G280 S281 A282 D284 I285 A291 N292
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0003862 3-isopropylmalate dehydrogenase activity
GO:0016491 oxidoreductase activity
GO:0016616 oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
GO:0046872 metal ion binding
GO:0051287 NAD binding
Biological Process
GO:0009098 L-leucine biosynthetic process
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:4xxv, PDBe:4xxv, PDBj:4xxv
PDBsum4xxv
PubMed
UniProtQ2T7H6|LEU3_BURTA 3-isopropylmalate dehydrogenase (Gene Name=leuB)

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