Structure of PDB 5hn6 Chain A

Receptor sequence
>5hn6A (length=329) Species: 69014 (Thermococcus kodakarensis KOD1) [Search protein sequence]
MYRVAVIPGDGIGPEVIDGAVRVLKAVTGRVRFEYYEGGVDVFQECGSPI
REEDLEEIRRSDAVLFGATTTPFDLPGYRSLILTLRKELGLYANLRIIPD
LRTGREIVIVRENSEGLYFGIGAVVNGRAVDVRLITREGAERIARFAVEQ
AKARGSFITFVHKANVLTGDKFFRRIVREVAGEEGVEVRDAIIDSFTIKL
VRNPWEHGVILSENLFGDILSDLATVHAGSIGIVPSGNYGDGIALFEPVH
GSAPDIAGKGIANPIGAILSGAMLLDYLGLDGSLIRAAVRGYVVNGELTP
DMGGRARTEDVVRGIIGEIEDLLSMDEVW
3D structure
PDB5hn6 Structure and function of an ancestral-type beta-decarboxylating dehydrogenase from Thermococcus kodakarensis
ChainA
Resolution2.5 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) Y118 K163 D194 D218 D222
Catalytic site (residue number reindexed from 1) Y118 K163 D194 D218 D222
Enzyme Commision number ?
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 A L83 R86 R96 R111 Y118 D218 L83 R86 R96 R111 Y118 D218
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0003862 3-isopropylmalate dehydrogenase activity
GO:0004449 isocitrate dehydrogenase (NAD+) 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:0006099 tricarboxylic acid cycle
GO:0006102 isocitrate metabolic process
GO:0009098 L-leucine biosynthetic process

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Molecular Function
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Biological Process
External links
PDB RCSB:5hn6, PDBe:5hn6, PDBj:5hn6
PDBsum5hn6
PubMed27831491
UniProtQ5JFV8

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