Structure of PDB 3vmk Chain B

Receptor sequence
>3vmkB (length=368) Species: 43661 (Shewanella benthica) [Search protein sequence]
HHHHGSSYQIAVLAGDGIGPEVMAEARKVLAAVEKRFDLSIEYSEYDVGG
AAIDNHGCPLPEATLKGCEAADAVLFGSVGGPKWEHLPPNDQPERGALLP
LRGHFELFCNMRPAKLHPGLEHMSPLRSDISEKGFDILCVRELTGGIYFG
KPKGRQGEGENEEAFDTMRYSRKEIRRIAKIAFESAQGRRKKVTSVDKAN
VLACSVLWREVVEEVAKDYPDVELEHIYIDNATMQLLRRPNEFDVMLCSN
LFGDIVSDEIAMLTGSMGLLASISMNSQGFGMYEPAGGSAPDIAGQGIAN
PVAQILSAALLLRHSLKLEDAALAIEAAVSKALSDGYLTCELLPASERSQ
AKSTSQMGDYIAQAIAEG
3D structure
PDB3vmk Structural analysis of 3-isopropylmalate dehydrogenase from the obligate piezophile Shewanella benthica DB21MT-2 and the nonpiezophile Shewanella oneidensis MR-1
ChainB
Resolution1.48 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) Y143 K193 D225 D249 D253
Catalytic site (residue number reindexed from 1) Y148 K198 D230 D254 D258
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 IPM B K193 N195 K198 N200
BS02 IPM B R97 R136 Y143 D249 R102 R141 Y148 D254
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:3vmk, PDBe:3vmk, PDBj:3vmk
PDBsum3vmk
PubMed22442218
UniProtD2YZL2

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