Structure of PDB 3aoe Chain A

Receptor sequence
>3aoeA (length=422) Species: 262724 (Thermus thermophilus HB27) [Search protein sequence]
SEPLSYLGKDGGPWEIFTEQVDRVVPYLGRLAPLAESLKRPKRVLIVDVP
VRLDDGSVAYFEGYRVHHNTARGPAKGGVRYHPEVTLSEVMALAGWMTIK
NAAVGLPYGGGKGGIRVDPRKLSPGELERLTRRYTSEIGILLGPDRDIPA
PDVNTGEREMAWMMDTYSMNVGRTVPGVVTGKPIALGGSLGRRDATGRGV
FITAAAAAEKIGLQVEGARVAIQGFGNVGNAAARAFHDHGARVVAVQDHT
GTVYNEAGIDPYDLLRHVQEFGGVRGYPKAEPLPAADFWGLPVEFLVPAA
LEKQITEQNAWRIRARIVAEGANGPTTPAADDILLEKGVLVVPDVIANAG
GVTVSYFEWVQDFNSYFWTEEEINARLERVLRNAFEAVWQVAQEKKIPLR
TAAYVVAATRVLEARALRGLYP
3D structure
PDB3aoe An unique allosteric regulation revealed by hetero-hexameric glutamate dehydrogenase from Thermus thermophilus
ChainA
Resolution2.6 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) K114 D154
Catalytic site (residue number reindexed from 1) K112 D152
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 A A73 R417 R420 G421 L422 Y423 A71 R415 R418 G419 L420 Y421
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

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

[Back to BioLiP]