Structure of PDB 4xxv Chain A

Receptor sequence
>4xxvA (length=356) Species: 271848 (Burkholderia thailandensis E264) [Search protein sequence]
HMKIAVLPGDGIGPEIVNEAVKVLNALDEKFELEHAPVGGAGYEASGHPL
PDATLALAKEADAILFGAVGDWKYDSLERALRPEQAILGLRKHLELFANF
RPAICYPQLVDASPLKPELVAGLDILIVRELNGDIYFGQPRGVRAAPDGP
FAGEREGFDTMRYSEPEVRRIAHVAFQAAQKRAKKLLSVDKSNVLETSQF
WRDVMIDVSKEYADVELSHMYVDNAAMQLAKAPKQFDVIVTGNMFGDILS
DEASMLTGSIGMLPSASLDKNNKGLYEPSHGSAPDIAGKGIANPLATILS
AAMLLRYSLNRAEQADRIERAVKTVLEQGYRTGDIATPGCRQVGTAAMGD
AVVAAL
3D structure
PDB4xxv Crystal structure of 3-isopropylmalate dehydrogenase from Burkholderia thailandensis in complex with NAD
ChainA
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) Y136 K191 D223 D247 D251
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 A N192 Y220 N223 N193 Y221 N224
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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