Structure of PDB 4xvx Chain B

Receptor sequence
>4xvxB (length=373) Species: 83332 (Mycobacterium tuberculosis H37Rv) [Search protein sequence]
SDLDDFRGLLAKAFDERVVAWTAEAEAQERFPRQLIEHLGVCGVFDAKWA
TDARPDVGKLVELAFALGQLASAGIGVGVSLHDSAIAILRRFGKSDYLRD
ICDQAIRGAAVLCIGASEESGGSDLQIVETEIRSRDGGFEVRGVKKFVSL
SPIADHIMVVARSVDHDPGNVAVVAVPAAQVSVQTPYRKVGAGPLDTAAV
CIDTWVPADALVARAGTGLAAISWGLAHERMSIAGQIAASCQRAIGITLA
RMMSRRQFGQTLFEHQALRLRMADLQARVDLLRYALHGIAEQGRLELRTA
AAVKVTAARLGEEVISECMHIFGGAGYLVDETTLGKWWRDMKLARVGGGT
DEVLWELVAAGMTPDHDGYAAVV
3D structure
PDB4xvx A covalent adduct of MbtN, an acyl-ACP dehydrogenase from Mycobacterium tuberculosis, reveals an unusual acyl-binding pocket.
ChainB
Resolution2.3 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) A120 S121 E237 G356 A368
Catalytic site (residue number reindexed from 1) A116 S117 E229 G348 A360
Enzyme Commision number 1.3.99.-
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 FDA B R263 Q265 F266 H273 L276 H328 I329 G332 R255 Q257 F258 H265 L268 H320 I321 G324
BS02 FDA B A120 S121 G126 S127 F151 S153 L351 T358 E360 A116 S117 G122 S123 F147 S149 L343 T350 E352
Gene Ontology
Molecular Function
GO:0003995 acyl-CoA dehydrogenase activity
GO:0016491 oxidoreductase activity
GO:0016627 oxidoreductase activity, acting on the CH-CH group of donors
GO:0050660 flavin adenine dinucleotide binding
GO:0141148 enoyl-[acyl-carrier-protein] reductase (NADPH) activity
Biological Process
GO:0019540 catechol-containing siderophore biosynthetic process
GO:0033539 fatty acid beta-oxidation using acyl-CoA dehydrogenase
Cellular Component
GO:0005737 cytoplasm

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Molecular Function
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Cellular Component
External links
PDB RCSB:4xvx, PDBe:4xvx, PDBj:4xvx
PDBsum4xvx
PubMed25849397
UniProtP9WQF9|MBTN_MYCTU Acyl-[acyl-carrier-protein] dehydrogenase MbtN (Gene Name=mbtN)

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