Structure of PDB 2x68 Chain A

Receptor sequence
>2x68A (length=350) Species: 294 (Pseudomonas fluorescens) [Search protein sequence]
TLDRVGVFAATHAAVAASDPLQARALVLQLPGLNRNKDVPGIVGLLREFL
PVRGLPSGWGFVEAAAAMRDIGFFLGSLKRHGHEPAEVVPGLEPVLLDLA
RATNLPPRETLLHVTVWNPTAADAQRSYTGLPDEAHLLESVRISMAALEA
AIALTVELFDVSLRSPEFAQRSDELEAYLQKMVESIVYAYRFISPQVFYD
ELRPFYEPIRVGGQSYLGPGAVEMPLFVLEHVLWGSQSDDQTYREFKETY
LPYVLPAYRAVYARFSGEPALIDRALDEARAVGTRDEHVRAGLTALERVF
KVLLRFRAPHLKLAERAYEVEIGSGGYAPSMLGELLTLTYAARSRVRAAL
3D structure
PDB2x68 The Ternary Complex of Prnb (the Second Enzyme in Pyrrolnitrin Biosynthesis Pathway), Tryptophan and Cyanide Yields New Mechanistic Insights Into the Indolamine Dioxygenase Superfamily.
ChainA
Resolution2.13 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 1.14.19.-
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 HEM A S188 I189 F201 A224 V225 M227 F249 F309 R310 H313 L316 G331 G333 Y335 L340 L343 S185 I186 F198 A221 V222 M224 F246 F306 R307 H310 L313 G323 G325 Y327 L332 L335
BS02 CTE A L140 F201 Y209 P222 G223 A224 Y321 G331 S332 L137 F198 Y206 P219 G220 A221 Y318 G323 S324 MOAD: Ka=21000M^-1
Gene Ontology
Molecular Function
GO:0016491 oxidoreductase activity
GO:0020037 heme binding
GO:0046872 metal ion binding
Biological Process
GO:0017000 antibiotic biosynthetic process
GO:0019441 tryptophan catabolic process to kynurenine

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Molecular Function
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Biological Process
External links
PDB RCSB:2x68, PDBe:2x68, PDBj:2x68
PDBsum2x68
PubMed20421301
UniProtP95481|PRNB_PSEFL Monodechloroaminopyrrolnitrin synthase PrnB (Gene Name=prnB)

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