Structure of PDB 3aoe Chain B

Receptor sequence
>3aoeB (length=424) Species: 262724 (Thermus thermophilus HB27) [Search protein sequence]
MKSEPLSYLGKDGGPWEIFTEQVDRVVPYLGRLAPLAESLKRPKRVLIVD
VPVRLDDGSVAYFEGYRVHHNTARGPAKGGVRYHPEVTLSEVMALAGWMT
IKNAAVGLPYGGGKGGIRVDPRKLSPGELERLTRRYTSEIGILLGPDRDI
PAPDVNTGEREMAWMMDTYSMNVGRTVPGVVTGKPIALGGSLGRRDATGR
GVFITAAAAAEKIGLQVEGARVAIQGFGNVGNAAARAFHDHGARVVAVQD
HTGTVYNEAGIDPYDLLRHVQEFGGVRGYPKAEPLPAADFWGLPVEFLVP
AALEKQITEQNAWRIRARIVAEGANGPTTPAADDILLEKGVLVVPDVIAN
AGGVTVSYFEWVQDFNSYFWTEEEINARLERVLRNAFEAVWQVAQEKKIP
LRTAAYVVAATRVLEARALRGLYP
3D structure
PDB3aoe An unique allosteric regulation revealed by hetero-hexameric glutamate dehydrogenase from Thermus thermophilus
ChainB
Resolution2.6 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) K114 D154
Catalytic site (residue number reindexed from 1) K114 D154
Enzyme Commision number 1.4.1.3: glutamate dehydrogenase [NAD(P)(+)].
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 LEU B A73 R417 R420 G421 Y423 A73 R417 R420 G421 Y423
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0004352 glutamate dehydrogenase (NAD+) activity
GO:0004353 glutamate dehydrogenase [NAD(P)+] activity
GO:0016491 oxidoreductase activity
GO:0016639 oxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor
Biological Process
GO:0006520 amino acid metabolic process
GO:0006538 glutamate catabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:3aoe, PDBe:3aoe, PDBj:3aoe
PDBsum3aoe
PubMed
UniProtQ72IC1

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