Structure of PDB 5ijz Chain J

Receptor sequence

>5ijzJ (length=447) Species: 196627 (Corynebacterium glutamicum ATCC 13032)

MTVDEQVSNYYDMLLKRNAGEPEFHQAVAEVLESLKIVLEKDPHYADYGL
IQRLCEPERQLIFRVPWVDDQGQVHVNRGFRVQFNSALGPYKGGLRFHPS
VNLGIVKFLGFEQIFKNSLTGLPIGGGKGGSDFDPKGKSDLEIMRFCQSF
MTELHRHIGEYRDVPAGDIGVGGREIGYLFGHYRRMANQHESGVLTGKGL
TWGGSLVRTEATGYGCVYFVSEMIKAKGESISGQKIIVSGSGNVATYAIE
KAQELGATVIGFSDSSGWVHTPNGVDVAKLREIKEVRRARVSVYADEVEG
ATYHTDGSIWDLKCDIALPCATQNELNGENAKTLADNGCRFVAEGANMPS
TPEAVEVFRERDIRFGPGKAANAGGVATSALEMQQNASRDSWSFEYTDER
LQVIMKNIFKTCAETAAEYGHENDYVVGANIAGFKKVADAMLAQGVI

3D structure

• PDB: 5ijz Structural insights into domain movement and cofactor specificity of glutamate dehydrogenase from Corynebacterium glutamicum
• Chain: J
• Resolution: 2.29 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): K128 D168
• Catalytic site (residue number reindexed from 1): K128 D168
• Enzyme Commision number: 1.4.1.4: glutamate dehydrogenase (NADP(+)).

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	NAP	J	R96 K116 D168 I169 S241 G242 N243 V244 S265 A321 N347	R96 K116 D168 I169 S241 G242 N243 V244 S265 A321 N347
BS02	AKG	J	K92 G94 Q113 K128 A166 G167 D168 S379	K92 G94 Q113 K128 A166 G167 D168 S379

Gene Ontology

Molecular Function

• GO:0004353 glutamate dehydrogenase [NAD(P)+] activity
• GO:0004354 glutamate dehydrogenase (NADP+) 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:0006537 glutamate biosynthetic process

Cellular Component

• GO:0005737 cytoplasm
• GO:0005829 cytosol

External links

• PDB: RCSB:5ijz, PDBe:5ijz, PDBj:5ijz
• PDBsum: 5ijz
• PubMed: 25727019
• UniProt: P31026|DHE4_CORGL NADP-specific glutamate dehydrogenase (Gene Name=gdh)