Structure of PDB 6hqd Chain A

Receptor sequence
>6hqdA (length=414) Species: 1084570 (Pseudomonas sp. 19-rlim) [Search protein sequence]
IDDAEIARSIALEDIDVSKPELFERDGLHPYFERLRREDPVHYCKASEYG
PYWSITKFSDIVAIDTNHKVFSSDHTNGSFVLDDTTLNAVDGGIYLPNFL
GMDPPKHDVHRMVVSPIVAPQNLLRFEATIRERTKRVLSELPIGEEFNWV
DRVSIELTTMMLATLLDFPFDDRRKLTRWSDIITTRPGYGLVDSWEQRES
ELMECLAYFQRLYAERQAMPPKPDLISMLAHSPEMQDLTPTDFLGTLALL
IVGGNDTTRSSMSGSAMACHLYPQEFDKVRNNRALLASVIPEVVRWQTPI
AHMRRTALEDVEFRGKQIRKGDKVVMWYLSGNRDDEVIDRPMDFIADRPR
ARHHLSFGFGIHRCLGNRLAELQLKILWEEMCERYSRIEVCGEPVRVPSN
LVHGYIDIPVRLHA
3D structure
PDB6hqd The Extreme Structural Plasticity in the CYP153 Subfamily of P450s Directs Development of Designer Hydroxylases.
ChainA
Resolution1.8 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) T191 D262 T263 C370 L371 G372
Catalytic site (residue number reindexed from 1) T185 D256 T257 C364 L365 G366
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 A D71 F105 L106 H113 R117 G259 G260 T263 Y334 S362 F363 H368 C370 G372 D65 F99 L100 H107 R111 G253 G254 T257 Y328 S356 F357 H362 C364 G366
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

[Back to BioLiP]