Structure of PDB 7mel Chain A

Receptor sequence
>7melA (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
PDB7mel Stereoselective synthesis of a 4-alpha-glucoside of valienamine and its X-ray structure in complex with Streptomyces coelicolor GlgE1-V279S.
ChainA
Resolution1.75 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 Z3D A K264 S279 W281 Q324 Y357 D359 R392 D394 N395 E423 D480 K534 Y535 K250 S265 W267 Q310 Y343 D345 R378 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:7mel, PDBe:7mel, PDBj:7mel
PDBsum7mel
PubMed34183716
UniProtQ9L1K2|GLGE1_STRCO Alpha-1,4-glucan:maltose-1-phosphate maltosyltransferase 1 (Gene Name=glgE1)

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