Structure of PDB 4u3c Chain E

Receptor sequence
>4u3cE (length=660) Species: 83331 (Mycobacterium tuberculosis CDC1551) [Search protein sequence]
PGRVEIDDVAPVVSCGVYPAKAVVGEVVPVSAAVWREGHEAVAATLVVRY
LGVRYPKPLLIPMTSGQEPFVFHGQFTPDRVGLWTFRVDGWGDPIHTWRH
GLIAKLDAGELSNDLLVGAVLLERAATGVPRGLRDPLLAAAAALRTPGDP
VTRTALALTPEIEELLADYPLRDLVTRGEQFGVWVDRPLARFGAWYEMFP
RSTGGWDDDGNPVHGTFATAAAELPRIAGMGFDVVYLPPIHPIGKVHRKG
RNNSPTAAPTDVGSPWAIGSDEGGHDTVHPSLGTIDDFDDFVSAARDLGM
EVALDLALQCAPDHPWAREHRQWFTELPDGTIAYAENPPKKYQDIYPLNF
DNDPEGLYDEVLRVVQHWVNHGVKFFRVDNPHTKPPNFWAWLIAQVKTVD
PDVLFLSEAFTPPARQYGLAKLGFTQSYSYFTWRTTKWELTEFGNQIAEL
ADYRRPNLFVNTPDILHAVLQHNGPGMFAIRAVLAATMSPAWGMYCGYEL
FEHRAVREGSEEYLDSEKYELRPRDFASALDQGRSLQPFITRLNIIRRLH
PAFQQLRTIHFHHVDNDALLAYSKFDPATGDCVLVVVTLNAFGPEEATLW
LDMAALGMEDYDRFWVRDEITGEEYQWGQANYIRIDPARAVAHIINMPAV
PYESRNTLLR
3D structure
PDB4u3c Crystal structures of Mycobacterium tuberculosis GlgE and complexes with non-covalent inhibitors.
ChainE
Resolution3.98 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 2.4.99.16: starch synthase (maltosyl-transferring).
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 GLC E D418 N419 D503 D379 N380 D464
BS02 GLC E K288 S303 D383 Y558 K249 S264 D344 Y519
BS03 GLC E T474 T475 K476 T435 T436 K437
BS04 GLC E K476 N629 K437 N590
BS05 GLC E N512 G513 P514 G515 A630 A677 N473 G474 P475 G476 A591 A638
Gene Ontology
Molecular Function
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
GO:0016757 glycosyltransferase activity
GO:0016758 hexosyltransferase activity
Biological Process
GO:0005975 carbohydrate metabolic process
GO:0005978 glycogen biosynthetic process
GO:0030979 alpha-glucan biosynthetic process

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Molecular Function
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Biological Process
External links
PDB RCSB:4u3c, PDBe:4u3c, PDBj:4u3c
PDBsum4u3c
PubMed26245983
UniProtP9WQ16|GLGE_MYCTO Alpha-1,4-glucan:maltose-1-phosphate maltosyltransferase (Gene Name=glgE)

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