Structure of PDB 5oeq Chain B

Receptor sequence
>5oeqB (length=417) Species: 83332 (Mycobacterium tuberculosis H37Rv) [Search protein sequence]
TTTATRLTGWGRTAPSVANVLRTPDAEMIVKAVARVAESGGGRGAIARGL
GRSYGDNAQNGGGLVIDMTPLNTIHSIDADTKLVDIDAGVNLDQLMKAAL
PFGLWVPVLPGTRQVTVGGAIACDIHGKNHHSAGSFGNHVRSMDLLTADG
EIRHLTPTGEDAELFWATVGGNGLTGIIMRATIEMTPTSTAYFIADGDVT
ASLDETIALHSDGSEARYTYSSAWFDAISAPPKLGRAAVSRGRLATVEQL
PAKLRSEPLKFDIGELWYRKSGTYRGKVQNLTQFYHGFLQYQFVIPTEAV
DEFKKIIGVIQASGHYSFLNVFKLFGPRNQAPLSFPIPGWNICVDFPIKD
GLGKFVSELDRRVLEFGGRLYTAKDSRTTAETFHAMYPRVDEWISVRRKV
DPLRVFASDMARRLELL
3D structure
PDB5oeq Determinants of the Inhibition of DprE1 and CYP2C9 by Antitubercular Thiophenes.
ChainB
Resolution2.25 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 1.1.98.3: decaprenylphospho-beta-D-ribofuranose 2-dehydrogenase.
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 W16 A53 G55 L56 G57 R58 S59 Y60 N63 A64 P116 G117 T118 V121 T122 G124 G125 A128 C129 I131 H132 N178 G179 I184 Y415 W10 A47 G49 L50 G51 R52 S53 Y54 N57 A58 P110 G111 T112 V115 T116 G118 G119 A122 C123 I125 H126 N172 G173 I178 Y371
Gene Ontology
Molecular Function
GO:0003885 D-arabinono-1,4-lactone oxidase activity
GO:0016491 oxidoreductase activity
GO:0050660 flavin adenine dinucleotide binding
GO:0071949 FAD binding
Biological Process
GO:0035884 arabinan biosynthetic process
GO:0045227 capsule polysaccharide biosynthetic process
GO:0046677 response to antibiotic
GO:0070592 cell wall polysaccharide biosynthetic process
GO:0071555 cell wall organization
Cellular Component
GO:0005886 plasma membrane
GO:0016020 membrane
GO:0042597 periplasmic space

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:5oeq, PDBe:5oeq, PDBj:5oeq
PDBsum5oeq
PubMed28815830
UniProtP9WJF1|DPRE1_MYCTU Decaprenylphosphoryl-beta-D-ribose oxidase (Gene Name=dprE1)

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