Structure of PDB 4u33 Chain B

Receptor sequence
>4u33B (length=661) Species: 83331 (Mycobacterium tuberculosis CDC1551) [Search protein sequence]
PGRVEIDDVAPVVSCGVYPAKAVVGEVVPVSAAVWREGHEAVAATLVVRY
LGVRYPHKPLLIPMTSGQEPFVFHGQFTPDRVGLWTFRVDGWGDPIHTWR
HGLIAKLDAGELSNDLLVGAVLLERAATGVPRGLRDPLLAAAAALRTPGD
PVTRTALALTPEIEELLADYPLRDLVTRGEQFGVWVDRPLARFGAWYEMF
PRSTGGWDDDGNPVHGTFATAAAELPRIAGMGFDVVYLPPIHPIGKVHRK
GRNNSPTAAPTDVGSPWAIGSDEGGHDTVHPSLGTIDDFDDFVSAARDLG
MEVALDLALQCAPDHPWAREHRQWFTELPDGTIAYAENPPKKYQDIYPLN
FDNDPEGLYDEVLRVVQHWVNHGVKFFRVDNPHTKPPNFWAWLIAQVKTV
DPDVLFLSEAFTPPARQYGLAKLGFTQSYSYFTWRTTKWELTEFGNQIAE
LADYRRPNLFVNTPDILHAVLQHNGPGMFAIRAVLAATMSPAWGMYCGYE
LFEHRAVREGSEEYLDSEKYELRPRDFASALDQGRSLQPFITRLNIIRRL
HPAFQQLRTIHFHHVDNDALLAYSKFDPATGDCVLVVVTLNAFGPEEATL
WLDMAALGMEDYDRFWVRDEITGEEYQWGQANYIRIDPARAVAHIINMPA
VPYESRNTLLR
3D structure
PDB4u33 Crystal structures of Mycobacterium tuberculosis GlgE and complexes with non-covalent inhibitors.
ChainB
Resolution3.293 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 B W305 Q348 D418 E447 D503 K557 W267 Q310 D380 E409 D465 K519
BS02 GLC B K288 S303 W305 Y381 D383 K557 Y558 K250 S265 W267 Y343 D345 K519 Y520
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

View graph for
Biological Process
External links
PDB RCSB:4u33, PDBe:4u33, PDBj:4u33
PDBsum4u33
PubMed26245983
UniProtP9WQ16|GLGE_MYCTO Alpha-1,4-glucan:maltose-1-phosphate maltosyltransferase (Gene Name=glgE)

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