Structure of PDB 3e2s Chain A

Receptor sequence

>3e2sA (length=468) Species: 83333 (Escherichia coli K-12)

QSVSRAAITAAYRRPETEAVSMLLEQARLPQPVAEQAHKLAYQLADKLRN
QKNASGRAGMVQGLLQEFSLSSQEGVALMCLAEALLRIPDKATRDALGEP
LIRKGVDMAMRLMGEQFVTGETIAEALANARKLEEKGFRYSYDMLGEAAL
TAADAQAYMVSYQQAIHAIGKASNGRGIYEGPGISIKLSALHPRYSRAQY
DRVMEELYPRLKSLTLLARQYDIGINIDAEESDRLEISLDLLEKLCFEPE
LAGWNGIGFVIQAYQKRCPLVIDYLIDLATRSRRRLMIRLVKGAYWDSEI
KRAQMDGLEGYPVYTRKVYTDVSYLACAKKLLAVPNLIYPQFATHNAHTL
AAIYQLAGQNYYPGQYEFQCLHGMGEPLYEQVTGKVADGKLNRPCRISAP
VGTHETLLAYLVRRLLENGANTSFVNRIADTSLPLDELVADPVTAVEKLA
QQEGQTGLPHPKIPLPRD

3D structure

• PDB: 3e2s A conserved active site tyrosine residue of proline dehydrogenase helps enforce the preference for proline over hydroxyproline as the substrate.
• Chain: A
• Resolution: 2.0 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	PRO	A	K329 L513 Y552 R555 R556	K187 L371 Y410 R413 R414
BS02	FAD	A	D370 A371 V402 Q404 V433 K434 G435 A436 Y437 W438 Y456 T457 R458 K459 T462 A485 T486 H487 N488 C512 L513 E559 S565 F566	D228 A229 V260 Q262 V291 K292 G293 A294 Y295 W296 Y314 T315 R316 K317 T320 A343 T344 H345 N346 C370 L371 E417 S423 F424

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:3e2s, PDBe:3e2s, PDBj:3e2s
• PDBsum: 3e2s
• PubMed: 19140736
• UniProt: P09546|PUTA_ECOLI Bifunctional protein PutA (Gene Name=putA)