Structure of PDB 5vp5 Chain A

Receptor sequence
>5vp5A (length=411) Species: 246196 (Mycolicibacterium smegmatis MC2 155) [Search protein sequence]
QPETLRRYRPGDPPLAGSLLIGGSGRVAEPLRTALADDYNLVSNNIGGRW
ADSFGGVVFDATGITEAEGLKELYTFFTPLLRNLAPCARVVVVGTTPAEA
GSVHAQVVQRALEGFTRSLGKELRRGATVSLVYLSADAKPGATGLESTMR
FILSAKSAYVDGQVFRVGAADSTPPADWDKPLDGKVAVVTGAARGIGATI
AEVFARDGATVVAIDVDGAAEDLKRVADKVGGTALTLDVTADDAVDKITA
HVTEHHGGKVDILVNNAGITRDKLLANMDEKRWDAVIAVNLLAPQRLTEG
LVGNGTIGEGGRVIGLSSMAGIAGNRGQTNYATTKAGMIGLAEALAPVLA
DKGITINAVAPGFIETRRLNSLFQGGQPVDVAELIAYFASPASNAVTGNT
IRVCGQAMLGA
3D structure
PDB5vp5 Crystal structure of a 3-oxoacyl-acyl-carrier protein reductase FabG4 from Mycobacterium smegmatis bound to NAD
ChainA
Resolution1.8 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) S343 Y356 K360
Catalytic site (residue number reindexed from 1) S318 Y331 K335
Enzyme Commision number 1.1.1.100: 3-oxoacyl-[acyl-carrier-protein] reductase.
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 NAD A G216 R219 I221 D240 V241 D263 V264 N291 A292 I294 S343 Y356 K360 P386 G191 R194 I196 D215 V216 D238 V239 N266 A267 I269 S318 Y331 K335 P361
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0016491 oxidoreductase activity
GO:0016616 oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
Biological Process
GO:0030497 fatty acid elongation

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Molecular Function
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Biological Process
External links
PDB RCSB:5vp5, PDBe:5vp5, PDBj:5vp5
PDBsum5vp5
PubMed38656226
UniProtA0QPE7

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