Structure of PDB 6hqg Chain A

Receptor sequence
>6hqgA (length=363) Species: 450851 (Phenylobacterium zucineum HLK1) [Search protein sequence]
DLQRAARDAAYSMPIEEINPADPELFRTDTMWPYFERLRKEDPVHWGVSP
HEDVGGYWSVTKYNDIMAVDTNHEVFSSEPTIVLPDPADDFTLPMFIAMD
PPKHDVQRKTVQPIVAPNHLAYLEPIIRERAGKILDDLPIGEEINWVDKV
SIELTTMTLATLFDFPWNLRRQTLFECVDYFMRLWNEMEYLGNLILLIVG
GNDTTRNTISGSVLALHQNPDQDRKLRENPGLIPAMVSETIRWQTPLAYM
RRRAKRDFELGGKTIREGDKVAMWYVSGNRDEEVIDRPNDYWIERPRVRQ
HLSFGFGVHRCVGNRLAELQLKIIWEEILARFPRLEVVGPPRRVYSSFVK
GYEELPVVIPTRN
3D structure
PDB6hqg The Extreme Structural Plasticity in the CYP153 Subfamily of P450s Directs Development of Designer Hydroxylases.
ChainA
Resolution2.9 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D265 T266 C373 V374 G375
Catalytic site (residue number reindexed from 1) D203 T204 C311 V312 G313
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 D76 F102 I103 G262 G263 T266 M312 R314 Y337 S365 F366 G367 H371 C373 V374 G375 A379 D70 F96 I97 G200 G201 T204 M250 R252 Y275 S303 F304 G305 H309 C311 V312 G313 A317
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:6hqg, PDBe:6hqg, PDBj:6hqg
PDBsum6hqg
PubMed30398864
UniProtB4RGA3

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