Structure of PDB 8dkq Chain A

Receptor sequence

>8dkqA (length=381) Species: 707241 (Sinorhizobium meliloti SM11)

QSTLRRAITAAYRRPETECLPPLVEAATQSKEIRDAAASTARKLIEALRG
KGEQFVTGETIREALKRSKELEEKGFSYSYDMLGEAATTAADAERYYRDY
ESAIHAIGKASAGRGIYEGPGISIKLSALHPRYSRAQAARVMGELLPRVK
ALALLAKNYDIGLNIDAEEADRLELSLDLLEVLCLDGDLSGWNGMGFVVQ
AYGKRCPFVLDFIIDLARRSGRRIMVRLVKGAYWDAEIKRAQLDGLADFP
VFTRKIHTDVSYIACAAKLLAATDVVFPQFATHNAQTLAAIYHMAGKDFH
VGKYEFQCLHGMGEPLYEEVVGRGKLDRPCRIYAPVGTHETLLAYLVRRL
LENGANSSFVHRINDPKVSIDELIADPVEVV

3D structure

• PDB: 8dkq Structure-based engineering of minimal proline dehydrogenase domains for inhibitor discovery.
• Chain: A
• Resolution: 1.72 Å

Enzymatic activity

• Enzyme Commision number: 1.2.1.88: L-glutamate gamma-semialdehyde dehydrogenase.
  1.5.5.2: proline dehydrogenase.

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	FAD	A	D306 A307 V338 Q340 R367 V369 K370 G371 A372 Y373 W374 F392 T393 R394 K395 T398 A421 T422 H423 N424 C448 L449 E492 S498 F499	D166 A167 V198 Q200 R227 V229 K230 G231 A232 Y233 W234 F252 T253 R254 K255 T258 A281 T282 H283 N284 C308 L309 E352 S358 F359
BS02	SJU	A	K265 D306 A372 L449 Y473 R488 R489	K125 D166 A232 L309 Y333 R348 R349

Gene Ontology

Molecular Function

• GO:0003842 1-pyrroline-5-carboxylate dehydrogenase activity
• GO:0004657 proline dehydrogenase activity

Biological Process

• GO:0006562 proline catabolic process

External links

• PDB: RCSB:8dkq, PDBe:8dkq, PDBj:8dkq
• PDBsum: 8dkq
• PubMed: 36448708
• UniProt: F7X6I3