Structure of PDB 1tj0 Chain A

Receptor sequence
>1tj0A (length=469) Species: 562 (Escherichia coli) [Search protein sequence]
QSVSRAAITAAYRRPETEAVSMLLEQARLPQPVAEQAHKLAYQLADKLRN
QKNASGRAGMVQGLLQEFSLSSQEGVALMCLAEALLRIPDKATRDALIRD
PLIRKGVDMAMRLMGEQFVTGETIAEALANARKLEEKGFRYSYDMLGEAA
LTAADAQAYMVSYQQAIHAIGKASNGRGIYEGPGISIKLSALHPRYSRAQ
YDRVMEELYPRLKSLTLLARQYDIGINIDAEESDRLEISLDLLEKLCFEP
ELAGWNGIGFVIQAYQKRCPLVIDYLIDLATRSRRRLMIRLVKGAYWDSE
IKRAQMDGLEGYPVYTRKVYTDVSYLACAKKLLAVPNLIYPQFATHNAHT
LAAIYQLAGQNYYPGQYEFQCLHGMGEPLYEQVTGKVADGKLNRPCRIYA
PVGTHETLLAYLVRRLLENGANTSFVNRIADTSLPLDELVADPVTAVEKL
AQQEGQTGLPHPKIPLPRD
3D structure
PDB1tj0 Structures of the Escherichia coli PutA proline dehydrogenase domain in complex with competitive inhibitors
ChainA
Resolution2.1 Å
3D
structure
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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 D229 A230 V261 Q263 R290 V292 K293 G294 A295 Y296 W297 Y315 T316 R317 K318 T321 A344 T345 H346 N347 Q370 C371 L372 E418 S424
Gene Ontology
Molecular Function
GO:0003842 1-pyrroline-5-carboxylate dehydrogenase activity
GO:0004657 proline dehydrogenase activity
Biological Process
GO:0006562 proline catabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:1tj0, PDBe:1tj0, PDBj:1tj0
PDBsum1tj0
PubMed15449943
UniProtP09546|PUTA_ECOLI Bifunctional protein PutA (Gene Name=putA)

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