Structure of PDB 4x4j Chain B

Receptor sequence
>4x4jB (length=480) Species: 797057 (Amycolatopsis orientalis subsp. vinearia) [Search protein sequence]
MDAPVVIAGAGPAGLMLAGELRLAGIGVVVLERLPARTGESRGLGFTART
MEVFDQRGLLRRFGEVQTSDQGHFGGIPVDFGLLDGAHQAAKTIPQSATE
AVLEAWAGELGADIRRGHELTGVRDDGDGVAVTVRGPAGEHVLRAGWLVG
CDGGRSAVRKAVGFDFPGTAATREMFLADLRGVELEPRSLPGGMVMVGPL
PGGVTRIIVCERDAPPRRRTGPPPFHEVADAWKRITGIDISAAEPVWLSA
FGDATRQVTEYRRGRVLLAGDAAHVHLPAGGQGMNAGIQDAVNLGWKLAA
VVRGTARADLLDTYHGERHPVGVRLLMNTRAQGLLFLNGAEMQPLRDVLA
ELTGYPDVARHLAAMVSGLEIAYDVGGGSHPWLGRRLPRLELDRPSSTAE
LLRPARGLLLDFAGNAALRDRAAPWAGRIDVVTARPAAGRVPGATTAVLV
RPDGHVAWAAPGTHADLPMALERWFGPAPR
3D structure
PDB4x4j Structural and Functional Studies of BexE: Insights into Oxidation During BE-7585A Biosynthesis
ChainB
Resolution2.65 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) L44 L204 I212 P282
Catalytic site (residue number reindexed from 1) L44 L200 I208 P278
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 FAD B G11 P12 A13 L31 E32 R33 L34 R42 G43 Q96 L120 D152 G153 D275 P282 G285 Q286 G287 M288 N289 G11 P12 A13 L31 E32 R33 L34 R42 G43 Q96 L120 D152 G153 D271 P278 G281 Q282 G283 M284 N285
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0016491 oxidoreductase activity
GO:0016709 oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen
GO:0071949 FAD binding

View graph for
Molecular Function
External links
PDB RCSB:4x4j, PDBe:4x4j, PDBj:4x4j
PDBsum4x4j
PubMed
UniProtD7RFJ3

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