Structure of PDB 6x9a Chain B

Receptor sequence

>6x9aB (length=1213) Species: 707241 (Sinorhizobium meliloti SM11)

APAPFADFAPPVRPQSTLRRAITAAYRRPETECLPPLVEAATQSKEIRDA
AASTARKLIEALRGKGVEGLVQEYSLSSQEGVALMCLAEALLRIPDTATR
DALIRDKIADGNWKSHLRSLFVNAATWGLVVTGKLTSTVNDRSLAAALTR
LISRCGEPVIRRGVDMAMRMMGEQFVTGETIREALKRSKELEEKGFSYSY
DMLGEAATTAADAERYYRDYESAIHAIGKASAGRGIYEGPGISIKLSALH
PRYSRAQAARVMGELLPRVKALALLAKNYDIGLNIDAEEADRLELSLDLL
EVLCLDGDLSGWNGMGFVVQAYGKRCPFVLDFIIDLARRSGRRIMVRLVK
GAYWDAEIKRAQLDGLADFPVFTRKIHTDVSYIACAAKLLAATDVVFPQF
ATHNAQTLAAIYHMAGKDFHVGKYEFQCLHGMGEPLYEEVVGRGKLDRPC
RIYAPVGTHETLLAYLVRRLLENGANSSFVHRINDPKVSIDELIADPVEV
VRAMPVVGAKHDRIALPAELFGDARTNSAGLDLSNEETLASLTEALRESA
AMKWTALPQLATGPAAGETRTVLNPGDHRDVVGSVTETSEEDARRAVRLA
ADAAPDWAAVPPSERAACLDRAAELMQARMPTLLGLIIREAGKSALNAIA
EVREAIDFLRYYAEQTRRTLGPGHGPLGPIVCISPWNFPLAIFTGQIAAA
LVAGNPVLAKPAEETPLIAAEGVRILREAGIPASALQLLPGDGRVGAALV
AAAETAGVMFTGSTEVARLIQAQLADRLSPAGRPIPLIAETGGQNAMIVD
SSALAEQVVGDVITSAFDSAGQRCSALRVLCLQEDVADRILTMLKGALHE
LHIGRTDRLSVDVGPVITSEAKDNIEKHIERMRGLGRKVEQIGLASETGV
GTFVPPTIIELEKLSDLQREVFGPVLHVIRYRRDDLDRLVDDVNATGYGL
TFGLHTRLDETIAHVTSRIKAGNLYINRNIIGAVVGVQPFGGRGLSGTGP
KAGGPLYLGRLVTTAPVPPQHSSVHTDPVLLDFAKWLDGKGARAEAEAAR
NAGSSSALGLDLELPGPVGERNLYTLHARGRILLVPATESGLYHQLAAAL
ATGNSVAIDAASGLQASLKNLPQTVGLRVSWSKDWAADGPFAGALVEGDA
ERIRAVNKAIAALPGPLLLVQAASSGEIARNPDAYCLNWLVEEVSASINT
AAAGGNASLMAIG

3D structure

• PDB: 6x9a Structural analysis of prolines and hydroxyprolines binding to the l-glutamate-gamma-semialdehyde dehydrogenase active site of bifunctional proline utilization A.
• Chain: B
• Resolution: 1.41 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): N707 K730 E810 C844 E940 A1022
• Catalytic site (residue number reindexed from 1): N687 K710 E790 C824 E920 A1002
• 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	B	D306 A307 V338 Q340 R367 V369 K370 G371 A372 Y373 W374 F392 T393 R394 K395 T398 A421 T422 H423 N424 C448 S498 F499	D286 A287 V318 Q320 R347 V349 K350 G351 A352 Y353 W354 F372 T373 R374 K375 T378 A401 T402 H403 N404 C428 S478 F479
BS02	UY7	B	E674 F708 S845 G1002 A1003 F1010	E654 F688 S825 G982 A983 F990	MOAD: Ki=4.5mM

Gene Ontology

Molecular Function

• GO:0000166 nucleotide binding
• GO:0003677 DNA binding
• GO:0003700 DNA-binding transcription factor activity
• GO:0003842 1-pyrroline-5-carboxylate dehydrogenase activity
• GO:0004657 proline dehydrogenase activity
• GO:0016491 oxidoreductase activity
• GO:0016620 oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor

Biological Process

• GO:0006355 regulation of DNA-templated transcription
• GO:0006560 proline metabolic process
• GO:0006561 proline biosynthetic process
• GO:0006562 proline catabolic process
• GO:0010133 proline catabolic process to glutamate

Cellular Component

• GO:0009898 cytoplasmic side of plasma membrane

External links

• PDB: RCSB:6x9a, PDBe:6x9a, PDBj:6x9a
• PDBsum: 6x9a
• PubMed: 33333077
• UniProt: F7X6I3