Structure of PDB 6hqd Chain C

Receptor sequence
>6hqdC (length=415) Species: 1084570 (Pseudomonas sp. 19-rlim) [Search protein sequence]
PIDDAEIARSIALEDIDVSKPELFERDGLHPYFERLRREDPVHYCKASEY
GPYWSITKFSDIVAIDTNHKVFSSDHTNGSFVLDDTTLNAVDGGIYLPNF
LGMDPPKHDVHRMVVSPIVAPQNLLRFEATIRERTKRVLSELPIGEEFNW
VDRVSIELTTMMLATLLDFPFDDRRKLTRWSDIITTRPGYGLVDSWEQRE
SELMECLAYFQRLYAERQAMPPKPDLISMLAHSPEMQDLTPTDFLGTLAL
LIVGGNDTTRSSMSGSAMACHLYPQEFDKVRNNRALLASVIPEVVRWQTP
IAHMRRTALEDVEFRGKQIRKGDKVVMWYLSGNRDDEVIDRPMDFIADRP
RARHHLSFGFGIHRCLGNRLAELQLKILWEEMCERYSRIEVCGEPVRVPS
NLVHGYIDIPVRLHA
3D structure
PDB6hqd The Extreme Structural Plasticity in the CYP153 Subfamily of P450s Directs Development of Designer Hydroxylases.
ChainC
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) T186 D257 T258 C365 L366 G367
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 C D71 F105 L106 H113 R117 G259 T263 P305 Y334 S362 F363 H368 C370 G372 A376 D66 F100 L101 H108 R112 G254 T258 P300 Y329 S357 F358 H363 C365 G367 A371
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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