Structure of PDB 3aog Chain E

Receptor sequence

>3aogE (length=421) Species: 262724 (Thermus thermophilus HB27)

EPLSYLGKDGGPWEIFTEQVDRVVPYLGRLAPLAESLKRPKRVLIVDVPV
RLDDGSVAYFEGYRVHHNTARGPAKGGVRYHPEVTLSEVMALAGWMTIKN
AAVGLPYGGGKGGIRVDPRKLSPGELERLTRRYTSEIGILLGPDRDIPAP
DVNTGEREMAWMMDTYSMNVGRTVPGVVTGKPIALGGSLGRRDATGRGVF
ITAAAAAEKIGLQVEGARVAIQGFGNVGNAAARAFHDHGARVVAVQDHTG
TVYNEAGIDPYDLLRHVQEFGGVRGYPKAEPLPAADFWGLPVEFLVPAAL
EKQITEQNAWRIRARIVAEGANGPTTPAADDILLEKGVLVVPDVIANAGG
VTVSYFEWVQDFNSYFWTEEEINARLERVLRNAFEAVWQVAQEKKIPLRT
AAYVVAATRVLEARALRGLYP

3D structure

• PDB: 3aog An unique allosteric regulation revealed by crystal structure of hetero-hexameric glutamate dehydrogenase from Thermus thermophilus
• Chain: E
• Resolution: 2.1 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): K114 D154
• Catalytic site (residue number reindexed from 1): K111 D151
• 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	GLU	E	D167 M171	D164 M168
BS02	GLU	E	G80 K114 P153 D154 V354 S357	G77 K111 P150 D151 V351 S354
BS03	GLU	E	A73 R420 G421 L422 Y423	A70 R417 G418 L419 Y420

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

External links

• PDB: RCSB:3aog, PDBe:3aog, PDBj:3aog
• PDBsum: 3aog
• UniProt: Q72IC1