Structure of PDB 5xwc Chain A

Receptor sequence

>5xwcA (length=459) Species: 5061 (Aspergillus niger)

SNLPHEPEFEQAYKELASTLENSTLFQKNPEYRKALAVVSVPERVIQFRV
VWEDDAGNVQVNRGFRVQFNSALGPYKGGLRFHPSVNLSILKFLGFEQIF
KNALTGLNMGGGKGGSDFDPKGKSDNEIRRFCVSFMTELCKHIGADTDVP
AGDIGVTGREVGFLFGQYRKIRNQWEGVLTGKGGSWGGSLIRPEATGYGV
VYYVEHMIAHATNGQESFKGKRVAISGSGNVAQYAALKVIELGGSVVSLS
DSQGSLIINGEGSFTPEEIELIAQTKVERKQLASIVGAAPFSDANKFKYI
AGARPWVHVGKVDVALPSATQNEISGEEAQVLINAGCKFIAEGSNMGCTQ
EAIDTFEAHRTANAGAAAIWYAPGKAANAGGVAVSGLEMAQNSARLSWTS
EEVDARLKDIMRDCFKNGLETAQEYATPAEGVLPSLVTGSNIAGFTKVAA
AMKDQGDWW

3D structure

• PDB: 5xwc Structural basis for the catalytic mechanism and alpha-ketoglutarate cooperativity of glutamate dehydrogenase.
• Chain: A
• Resolution: 1.75 Å

Enzymatic activity

• 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	A	H84 K122 D154 I155 R193 T197 S229 G230 N231 V232 D252 S253 A320 T321 G344 S345 N346 N379	H83 K121 D153 I154 R192 T196 S228 G229 N230 V231 D251 S252 A319 T320 G343 S344 N345 N378
BS02	8GL	A	K78 G79 G80 Q99 K102 K114 A152 D154 R193 V383 S386	K77 G78 G79 Q98 K101 K113 A151 D153 R192 V382 S385
BS03	2IT	A	K78 G79 Q99 K102 K114 A152 R193 V383 S386	K77 G78 Q98 K101 K113 A151 R192 V382 S385

Gene Ontology

Molecular Function

• GO:0000166 nucleotide binding
• 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:0005829 cytosol

External links

• PDB: RCSB:5xwc, PDBe:5xwc, PDBj:5xwc
• PDBsum: 5xwc
• PubMed: 29540480
• UniProt: B6V7E4