Structure of PDB 3rwl Chain A

Receptor sequence
>3rwlA (length=404) Species: 33050 (Sphingopyxis macrogoltabida) [Search protein sequence]
QSAAATMPLDSIDVSIPELFYNDSVGEYFKRLRKDDPVHYCADSAFGPYW
SITKYNDIMHVDTNHDIFSSDAGYGGIIIDDGILDLPNFIAMDRPRHDEQ
RKAVSPIVAPANLAALEGTIRERVSKTLDGLPVGEEFDWVDRVSIEITTQ
MLATLFDFPFEERRKLTRWSDVTTAAPGGGVVESWDQRKTELLECAAYFQ
VLWNERVNKDPGNDLISMLAHSPATRNMTPEEYLGNVLLLIVGGNDTTRN
SMTGGVLALHKNPDQFAKLKANPALVETMVPEIIRWQTPLAHMRRTAIAD
SELGGKTIRKGDKVVMWYYSGNRDDEVIDRPEEFIIDRPRPRQHLSFGFG
IHRCVGNRLAEMQLRILWEEILTRFSRIEVMAEPERVRSNFVRGYAKMMV
RVHA
3D structure
PDB3rwl Evolving P450pyr hydroxylase for highly enantioselective hydroxylation at non-activated carbon atom.
ChainA
Resolution2.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) A187 G255 D258 T259 T260 C366 V367 G368 Q375 V404
Catalytic site (residue number reindexed from 1) A175 G243 D246 T247 T248 C354 V355 G356 Q363 V392
Enzyme Commision number 1.14.15.3: alkane 1-monooxygenase.
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 D67 F101 I102 H109 L251 L252 G255 G256 T259 P301 L302 Y330 S358 F359 G360 H364 C366 V367 G368 D62 F89 I90 H97 L239 L240 G243 G244 T247 P289 L290 Y318 S346 F347 G348 H352 C354 V355 G356
Gene Ontology
Molecular Function
GO:0004497 monooxygenase activity
GO:0005506 iron ion binding
GO:0016705 oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
GO:0018685 alkane 1-monooxygenase activity
GO:0020037 heme binding
GO:0046872 metal ion binding
GO:0120250 fatty acid omega-hydroxylase activity

View graph for
Molecular Function
External links
PDB RCSB:3rwl, PDBe:3rwl, PDBj:3rwl
PDBsum3rwl
PubMed22430002
UniProtQ5F4D9

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