Structure of PDB 4aut Chain A

Receptor sequence
>4autA (length=419) Species: 1772 (Mycolicibacterium smegmatis) [Search protein sequence]
FPTTTKRLMGWGRTAPTVASVLSTSDPEVIVRAVTRAAEEGGRGVIARGL
GRSYGDNAQNGGGLVIDMPALNRIHSIDSGTRLVDVDAGVSLDQLMKAAL
PHGLWVPVLPGTRQVTVGGAIGCDIHGKNHHSAGSFGNHVRSMELLTANG
EVRHLTPAGPDSDLFWATVGGNGLTGIILRATIEMTPTETAYFIADGDVT
GSLDETIAFHSDGSEANYTYSSAWFDAISKPPKLGRAAISRGSLAKLDQL
PSKLQKDPLKFYRKSGTYRNKVQNLTQFYHPLDMFGEAGFLQYQFVVPTE
AVEEFKSIIVDIQRSGHYSFLNVFKLFGPGNQAPLSFPIPGWNVCVDFPI
KAGLHEFVTELDRRVLEFGGRLYTAKDSRTTAETFHAMYPRIDEWIRIRR
SVDPDGVFASDMARRLQLL
3D structure
PDB4aut Structural Basis for Benzothiazinone-Mediated Killing of Mycobacterium Tuberculosis.
ChainA
Resolution2.1 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 A W24 I59 A60 G62 L63 G64 R65 S66 Y67 N70 A71 M81 P123 G124 T125 T129 G131 G132 C136 I138 H139 N185 G186 I191 Y422 W11 I46 A47 G49 L50 G51 R52 S53 Y54 N57 A58 M68 P110 G111 T112 T116 G118 G119 C123 I125 H126 N172 G173 I178 Y373
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
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:0045227 capsule polysaccharide biosynthetic process
GO:0046677 response to antibiotic
GO:0071555 cell wall organization
Cellular Component
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:4aut, PDBe:4aut, PDBj:4aut
PDBsum4aut
PubMed22956199
UniProtA0R607|DPRE1_MYCS2 Decaprenylphosphoryl-beta-D-ribose oxidase (Gene Name=dprE1)

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