Structure of PDB 2wet Chain A

Receptor sequence
>2wetA (length=496) Species: 295838 (Streptomyces rugosporus) [Search protein sequence]
MIRSVVIVGGGTAGWMTASYLKAAFDDRIDVTLVESGNVRRIGVGEATFS
TVRHFFDYLGLDEREWLPRCAGGYKLGIRFENWSEPGEYFYHPFERLRVV
DGFNMAEWWLAVGTSFSEACYLTHRLCEAKRAPRMLDGSLFASEQRAQFP
YAYHFDADEVARYLSEYAIARGVRHVVDDVQHVGQDERGWISGVHTKQHG
EISGDLFVDCTGFRGLLINQTLGGRFQSFSDVLPNNRAVALRVPRENDED
MRPYTTATAMSAGWMWTIPLFKRDGNGYVYSDEFISPEEAERELRSTVAP
GRDDLEANHIQMRIGRNERTWINNCVAVGLSAAFVEPLESTGIFFIQHAI
EQLVKHFPGERWDPVLISAYNERMAHMVDGVKEFLVLHYKGAQREDTPYW
KAAKTRAMPDGLARKLELSASHLLDEQTIYPYYHGFETYSWITMNLGLGI
VPERPRPALLHMDPAPALAEFERLRREGDELIAALPSCYEYLASIQ
3D structure
PDB2wet Structural Insights in the Regioselectivity in the Enzymatic Chlorination of Tryptophan.
ChainA
Resolution2.4 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 1.14.19.58: tryptophan 5-halogenase.
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 G9 G10 G11 T12 A13 E35 S36 V39 R41 I42 V44 G45 A47 V195 C225 T226 L345 F349 P352 G357 I358 I361 G9 G10 G11 T12 A13 E35 S36 V39 R41 I42 V44 G45 A47 V180 C210 T211 L330 F334 P337 G342 I343 I346
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0003824 catalytic activity
GO:0004497 monooxygenase activity
GO:0016491 oxidoreductase activity
Biological Process
GO:0017000 antibiotic biosynthetic process

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Molecular Function
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Biological Process
External links
PDB RCSB:2wet, PDBe:2wet, PDBj:2wet
PDBsum2wet
PubMed19501593
UniProtA4D0H5|TRP5H_STRRG Tryptophan 5-halogenase PyrH (Gene Name=pyrH)

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