Structure of PDB 7mgy Chain B

Receptor sequence
>7mgyB (length=649) Species: 100226 (Streptomyces coelicolor A3(2)) [Search protein sequence]
PTVVGRIPVLDVRPVVQRGRRPAKAVTGESFEVSATVFREGHDAVGANVV
LRDPRGRPGPWTPMRELAPGTDRWGATVTAGETGTWSYTVEAWGDPVTTW
RHHARIKIPAGLDTDLVLEEGARLYERAAADVPGREDRRELLAAVDALRD
ESRPAASRLAAALTPQVDAVLARHPLRDLVTSSDPLPLLVERERALYGAW
YEFFPRSEGTPHTPHGTFRTAARRLPAIAAMGFDVVYLPPIHPIGTTHRK
GRNNTLSATGDDVGSPWAIGSPEGGHDSIHPALGTLDDFDHFVTEAGKLG
LEIALDFALQCSPDHPWVHKHPEWFHHRPDGTIAHAENPPKKYQDIYPIA
FDADPDGLATETVRILRHWMDHGVRIFRVDNPHTKPVAFWERVIADINGT
DPDVIFLAEAFTRPAMMATLAQIGFQQSYTYFTWRNTKQELTEYLTELSG
EAASYMRPNFFANTPDILHAYLQHGGRPAFEVRAVLAATLSPTWGIYSGY
ELCENTPLREGSEEYLDSEKYQLKPRDWTRAAREGTTIAPLVTRLNTIRR
ENPALRQLRDLHFHPTDKEEVIAYSKRQGSNTVLVVVNLDPRHTQEATVS
LDMPQLGLDWHESVPVRDELTGETYHWGRANYVRLEPGRTPAHVCTVLR
3D structure
PDB7mgy Stereoselective synthesis of a 4-⍺-glucoside of valienamine and its X-ray structure in complex with Streptomyces coelicolor GlgE1-V279S.
ChainB
Resolution1.83 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 ZD1 B K264 S279 W281 Q324 Y357 D359 D394 N395 E423 D480 K534 Y535 K250 S265 W267 Q310 Y343 D345 D380 N381 E409 D466 K520 Y521
Gene Ontology
Molecular Function
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
GO:0004556 alpha-amylase activity
GO:0016757 glycosyltransferase activity
GO:0016758 hexosyltransferase activity
Biological Process
GO:0005975 carbohydrate metabolic process
GO:0009313 oligosaccharide catabolic process
GO:0030979 alpha-glucan biosynthetic process

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Molecular Function
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Biological Process
External links
PDB RCSB:7mgy, PDBe:7mgy, PDBj:7mgy
PDBsum7mgy
PubMed34183716
UniProtQ9L1K2|GLGE1_STRCO Alpha-1,4-glucan:maltose-1-phosphate maltosyltransferase 1 (Gene Name=glgE1)

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