Structure of PDB 6hqg Chain B

Receptor sequence
>6hqgB (length=364) Species: 450851 (Phenylobacterium zucineum HLK1) [Search protein sequence]
DLQRAARDAAYSMPIEEINPADPELFRTDTMWPYFERLRKEDPVHWGVSP
HEDVGGYWSVTKYNDIMAVDTNHEVFSSEPTIVLPDPADDFTLPMFIAMD
PPKHDVQRKTVQPIVAPNHLAYLEPIIRERAGKILDDLPIGEEINWVDKV
SIELTTMTLATLFDFPWENLRRQTLFECVDYFMRLWNEMEYLGNLILLIV
GGNDTTRNTISGSVLALHQNPDQDRKLRENPGLIPAMVSETIRWQTPLAY
MRRRAKRDFELGGKTIREGDKVAMWYVSGNRDEEVIDRPNDYWIERPRVR
QHLSFGFGVHRCVGNRLAELQLKIIWEEILARFPRLEVVGPPRRVYSSFV
KGYEELPVVIPTRN
3D structure
PDB6hqg The Extreme Structural Plasticity in the CYP153 Subfamily of P450s Directs Development of Designer Hydroxylases.
ChainB
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) D204 T205 C312 V313 G314
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 D76 F102 I103 H110 L259 G262 G263 T266 I303 M312 R314 Y337 S365 F366 G367 H371 C373 V374 G375 D70 F96 I97 H104 L198 G201 G202 T205 I242 M251 R253 Y276 S304 F305 G306 H310 C312 V313 G314
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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