Structure of PDB 7ecr Chain B

Receptor sequence
>7ecrB (length=460) Species: 33178 (Aspergillus terreus) [Search protein sequence]
MSNLPVEPEFEQAYKELASTLENSTLFQKNPEYRKALAVVSVPERVIQFR
VVWENDKGEVQVNRGFRVQFNSALGPYKGGLRFHPSVNLSILKFLGFEQI
FKNALTGLNMGGGKGGSDFDPKGKSDSEIRRFCVAFMTELCRHIGADTDV
PAGDIGVTGREIGYLFGQYRKLRNSWEGVLTGKGGSWGGSLIRPEATGYG
VVYYVEHMIAHATNGAESFAGKRVAISGSGNVAQYAALKVIELGGRVVSL
SDSQGSLIVKDTAKDSFTPAEIDAIAALKVDRKQIAELVTDAAFADKFTY
LPGQRPWVHVGAVDVALPSATQNEVSGEEAQALIAAGCKFIAEGSNMGCT
QAAIDAFEAHREANKGAAAIWYAPGKAANAGGVAVSGLEMAQNSARLSWT
AEEVDARLKDIMKSCFQNGLDTAKEYATPADGILPSLVTGSNIAGFTKVA
AAMKDQGDWW
3D structure
PDB7ecr Molecular insights into the inhibition of glutamate dehydrogenase by the dicarboxylic acid metabolites.
ChainB
Resolution1.73 Å
3D
structure
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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 A2R B K122 D154 I155 S229 G230 N231 V232 D252 S253 K279 A320 T321 S345 N346 N379 K122 D154 I155 S229 G230 N231 V232 D252 S253 K279 A320 T321 S345 N346 N379
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

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Biological Process
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Cellular Component
External links
PDB RCSB:7ecr, PDBe:7ecr, PDBj:7ecr
PDBsum7ecr
PubMed34748226
UniProtT2D1F5

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