Structure of PDB 6hqd Chain B

Receptor sequence
>6hqdB (length=412) Species: 1084570 (Pseudomonas sp. 19-rlim) [Search protein sequence]
DAEIARSIALEDIDVSKPELFERDGLHPYFERLRREDPVHYCKASEYGPY
WSITKFSDIVAIDTNHKVFSSDHTNGSFVLDDTTLNAVDGGIYLPNFLGM
DPPKHDVHRMVVSPIVAPQNLLRFEATIRERTKRVLSELPIGEEFNWVDR
VSIELTTMMLATLLDFPFDDRRKLTRWSDIITTRPGYGLVDSWEQRESEL
MECLAYFQRLYAERQAMPPKPDLISMLAHSPEMQDLTPTDFLGTLALLIV
GGNDTTRSSMSGSAMACHLYPQEFDKVRNNRALLASVIPEVVRWQTPIAH
MRRTALEDVEFRGKQIRKGDKVVMWYLSGNRDDEVIDRPMDFIADRPRAR
HHLSFGFGIHRCLGNRLAELQLKILWEEMCERYSRIEVCGEPVRVPSNLV
HGYIDIPVRLHA
3D structure
PDB6hqd The Extreme Structural Plasticity in the CYP153 Subfamily of P450s Directs Development of Designer Hydroxylases.
ChainB
Resolution1.8 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) T191 D262 T263 C370 L371 G372
Catalytic site (residue number reindexed from 1) T183 D254 T255 C362 L363 G364
Enzyme Commision number ?
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 B D71 F105 L106 H113 R117 G259 T263 P305 Y334 S362 F363 H368 C370 G372 D63 F97 L98 H105 R109 G251 T255 P297 Y326 S354 F355 H360 C362 G364
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:0020037 heme binding
GO:0046872 metal ion binding

View graph for
Molecular Function
External links
PDB RCSB:6hqd, PDBe:6hqd, PDBj:6hqd
PDBsum6hqd
PubMed30398864
UniProtG3LGZ6

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