Structure of PDB 2v7l Chain A

Receptor sequence
>2v7lA (length=344) Species: 294 (Pseudomonas fluorescens) [Search protein sequence]
TLDRVGVFAATHAAVAASDPLQARALVLQLPGLNRNKDVPGIVGLLREFL
PVRGLPSGWGFVEAAAAMRDIGFFLGSLKRHGHEPAEVVPGLEPVLLDLA
RATNLPPRETLLHVTVWNPTAADAQRSYTGLPDEAHLLESVRISMAALEA
AIALTVELFDVSLRSPEFAQRSDELEAYLQKMVESIVYAYRFISPQVFYD
ELRPFYEPIRVGGQSYLGPGAVEMPLFVLEHVLWGSQSDDQTYREFKETY
LPYVLPAYRAVYARFSGEPALIDRALDEARAVGTRDEHVRAGLTALERVF
KVLLRFRAPHLKLAERAYEVAPSMLGELLTLTYAARSRVRAALD
3D structure
PDB2v7l The Second Enzyme in Pyrrolnitrin Biosynthetic Pathway is Related to the Heme-Dependent Dioxygenase Superfamily.
ChainA
Resolution2.4 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 S143 S188 I189 F201 A224 V225 M227 L229 F309 R310 H313 L316 A317 P337 M339 L340 L343 S140 S185 I186 F198 A221 V222 M224 L226 F306 R307 H310 L313 A314 P322 M324 L325 L328
BS02 CTE A L140 V144 F201 Y209 G223 A224 V225 L137 V141 F198 Y206 G220 A221 V222
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:2v7l, PDBe:2v7l, PDBj:2v7l
PDBsum2v7l
PubMed17924666
UniProtP95481|PRNB_PSEFL Monodechloroaminopyrrolnitrin synthase PrnB (Gene Name=prnB)

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