Structure of PDB 3q1g Chain B

Receptor sequence
>3q1gB (length=468) Species: 59406 (Aromatoleum evansii) [Search protein sequence]
ERIPNNVNLNENKTLQRALEQWQPSFLNWWDDMGPENSSNYDVYLRTAVS
VDPKGWADFGYVKMHDYRWGIFLAPQEGEKKITFGEHKGQDVWQEVPGEY
RSTLRRIIVTQGDTEPASVEQQRHLGLTAPSLYDLRNLFQVNVEEGRHLW
AMVYLLHAHFGRDGREEGEALLERRSGDEDNPRILTAFNEKTPDWLSFFM
FTFITDRDGKFQLASLAESAFDPLARTCKFMLTEEAHHLFVGESGIARVI
QRTCEVMKELGTDDPAKLRAAGVIDLPTLQKYLNFHYSVTSDLYGAEISS
NAATYYTNGLKGRFEEEKIGDDHKLQNSEYEVMDVAGDKILTRHVPALSA
LNERLRDDWITDVQAGVDRWNRIPAKFGFDFRFTLPHKGFHRKIGMFADV
HVSPDGRLISEAEWTHQHKNWLPTESDRLYVHSLMGRCLEPGKFANWIAA
PARGINNQPVNFEYVRFN
3D structure
PDB3q1g Structure and Mechanism of the Diiron Benzoyl-Coenzyme A Epoxidase BoxB.
ChainB
Resolution2.5 Å
3D
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
Enzyme Commision number 1.14.13.208: benzoyl-CoA 2,3-epoxidase.
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 FE B E120 E150 H153 E240 E115 E145 H148 E235
BS02 FE B E150 D211 E240 H243 E145 D206 E235 H238
Gene Ontology
Molecular Function
GO:0016491 oxidoreductase activity
GO:0046872 metal ion binding
GO:0051213 dioxygenase activity
Biological Process
GO:0009056 catabolic process
GO:0010124 phenylacetate catabolic process
Cellular Component
GO:0005829 cytosol

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:3q1g, PDBe:3q1g, PDBj:3q1g
PDBsum3q1g
PubMed21632537
UniProtQ9AIX7|BOXB_AROEV Benzoyl-CoA oxygenase component B (Gene Name=boxB)

[Back to BioLiP]