Structure of PDB 3aog Chain K

Receptor sequence

>3aogK (length=416) Species: 262724 (Thermus thermophilus HB27)

EPLSYLGKDGGPWEIFTEQVDRVVPYLGRLAPLAESLKRPKRVLIVDVPV
RLDDGSVAYFEGYRVHHNTARGPAKGGVRYHPEVTLSEVMALAGWMTIKN
AAVGLPYGGGKGGIRVDPRKLSPGELERLTRRYTSEIGILLGPDRDIPAP
DVNTGEREMAWMMDTYSMNVGRTVPGVVTGKPIALGGSLGRRDATGRGVF
ITAAAAAEKIGLQVEGARVAIQGFGNVGNAAARAFHDHGARVVAVQDHTG
TVYNEAGIDPYDLLRHVQEFGGVRGYPKAEPLPAADFWGLPVEFLVPAAL
EKQITEQNARIVAEGANGPTTPAADDILLEKGVLVVPDVIANAGGVTVSY
FEWVQDFNSYFWTEEEINARLERVLRNAFEAVWQVAQEKKIPLRTAAYVV
AATRVLEARALRGLYP

3D structure

• PDB: 3aog An unique allosteric regulation revealed by crystal structure of hetero-hexameric glutamate dehydrogenase from Thermus thermophilus
• Chain: K
• 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	K	G80 M99 K114 P153 R194 G353 S357	G77 M96 K111 P150 R191 G345 S349
BS02	GLU	K	A73 R420 G421 L422 Y423	A70 R412 G413 L414 Y415
BS03	GLU	K	D167 M171	D164 M168

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