Structure of PDB 3zt5 Chain A

Receptor sequence
>3zt5A (length=649) Species: 1902 (Streptomyces coelicolor) [Search protein sequence]
PTVVGRIPVLDVRPVVQRGRRPAKAVTGESFEVSATVFREGHDAVGANVV
LRDPRGRPGPWTPMRELAPGTDRWGATVTAGETGTWSYTVEAWGDPVTTW
RHHARIKIPAGLDTDLVLEEGARLYERAAADVPGREDRRELLAAVDALRD
ESRPAASRLAAALTPQVDAVLARHPLRDLVTSSDPLPLLVERERALYGAW
YEFFPRSEGTPHTPHGTFRTAARRLPAIAAMGFDVVYLPPIHPIGTTHRK
GRNNTLSATGDDVGVPWAIGSPEGGHDSIHPALGTLDDFDHFVTEAGKLG
LEIALDFALQCSPDHPWVHKHPEWFHHRPDGTIAHAENPPKKYQDIYPIA
FDADPDGLATETVRILRHWMDHGVRIFRVDNPHTKPVAFWERVIADINGT
DPDVIFLAEAFTRPAMMATLAQIGFQQSYTYFTWRNTKQELTEYLTELSG
EAASYMRPNFFANTPDILHAYLQHGGRPAFEVRAVLAATLSPTWGIYSGY
ELCENTPLREGSEEYLDSEKYQLKPRDWTRAAREGTTIAPLVTRLNTIRR
ENPALRQLRDLHFHPTDKEEVIAYSKRQGSNTVLVVVNLDPRHTQEATVS
LDMPQLGLDWHESVPVRDELTGETYHWGRANYVRLEPGRTPAHVCTVLR
3D structure
PDB3zt5 Structure of a Streptomyces Maltosyltransferase Glge: A Homologue of a Genetically Validated Anti-Tuberculosis Target.
ChainA
Resolution2.09 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 A W281 Q324 D394 N395 E423 D480 W267 Q310 D380 N381 E409 D466
BS02 GLC A K264 V279 W281 A282 Y357 D359 K534 Y535 K250 V265 W267 A268 Y343 D345 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:3zt5, PDBe:3zt5, PDBj:3zt5
PDBsum3zt5
PubMed21914799
UniProtQ9L1K2|GLGE1_STRCO Alpha-1,4-glucan:maltose-1-phosphate maltosyltransferase 1 (Gene Name=glgE1)

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