Structure of PDB 1tj2 Chain A

Receptor sequence

>1tj2A (length=450) Species: 562 (Escherichia coli)

QSVSRAAITAAYRRPETEAVSMLLEQARLPQPVAEQAHKLAYQLADKLRN
QKNASGRAGMGVALMCLAEALLRIPDKATRDALIRKGVDMAMRLMGEQFV
TGETIAEALANARKLEEKGFRYSYDMLGEAALTAADAQAYMVSYQQAIHA
IGKASNGRGIYEGPGISIKLSALHPRYSRAQYDRVMEELYPRLKSLTLLA
RQYDIGINIDAEESDRLEISLDLLEKLCFEPELAGWNGIGFVIQAYQKRC
PLVIDYLIDLATRSRRRLMIRLVKGAYWDSEIKRAQMDGLEGYPVYTRKV
YTDVSYLACAKKLLAVPNLIYPQFATHNAHTLAAIYQLAGQNYYPGQYEF
QCLHGMGEPLYEQVTGKVADGKLNRPCRIYAPVGTHETLLAYLVRRLLEN
GANTSFVNRIADTSLPLDELVADPVTAVEKLAQQEGQTGLPHPKIPLPRD

3D structure

• PDB: 1tj2 Structures of the Escherichia coli PutA proline dehydrogenase domain in complex with competitive inhibitors
• Chain: A
• Resolution: 2.05 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	ACT	A	K329 Y552 R555 R556	K169 Y392 R395 R396	MOAD: Ki=30mM
BS02	FAD	A	D370 A371 V402 Q404 R431 V433 K434 G435 A436 Y437 W438 Y456 T457 R458 K459 T462 A485 T486 H487 N488 Q511 C512 L513 E559 S565	D210 A211 V242 Q244 R271 V273 K274 G275 A276 Y277 W278 Y296 T297 R298 K299 T302 A325 T326 H327 N328 Q351 C352 L353 E399 S405

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:1tj2, PDBe:1tj2, PDBj:1tj2
• PDBsum: 1tj2
• PubMed: 15449943
• UniProt: P09546|PUTA_ECOLI Bifunctional protein PutA (Gene Name=putA)