Structure of PDB 2fzn Chain A

Receptor sequence

>2fznA (length=449) Species: 562 (Escherichia coli)

QSVSRAAITAAYRRPETEAVSMLLEQARLPQPVAEQAHKLAYQLADKLRN
QKNASGRAGGVALMCLAEALLRIPDKATRDALIRKGVDMAMRLMGEQFVT
GETIAEALANARKLEEKGFRYSYDMLGEAALTAADAQAYMVSYQQAIHAI
GKASNGRGIYEGPGISIKLSALHPRYSRAQYDRVMEELYPRLKSLTLLAR
QYDIGINIDAEESDRLEISLDLLEKLCFEPELAGWNGIGFVIQAYQKRCP
LVIDYLIDLATRSRRRLMIRLVKGAYWDSEIKRAQMDGLEGYPVYTRKVY
TDVSYLACAKKLLAVPNLIYPQFATHNAHTLAAIYQLAGQNYYPGQYEFQ
CLHGMGEPLYEQVTGKVADGKLNRPCRIYAPVGTHETLLAYLVRRLLENG
ANTSFVNRIADTSLPLDELVADPVTAVEKLAQQEGQTGLPHPKIPLPRD

3D structure

• PDB: 2fzn Hydrogen Bonding Interactions of the 2-OH Ribityl Group and the N(5) Position of the FAD Cofactor Regulate PutA-membrane Associations in Escherichia coli
• 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	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	D209 A210 V241 Q243 R270 V272 K273 G274 A275 Y276 W277 Y295 T296 R297 K298 T301 A324 T325 H326 N327 Q350 C351 L352 E398 S404
BS02	PRO	A	K329 L513 Y540 R555 R556	K168 L352 Y379 R394 R395

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:2fzn, PDBe:2fzn, PDBj:2fzn
• PDBsum: 2fzn
• UniProt: P09546|PUTA_ECOLI Bifunctional protein PutA (Gene Name=putA)