Structure of PDB 5e6y Chain B

Receptor sequence
>5e6yB (length=594) Species: 331111 (Escherichia coli O139:H28 str. E24377A) [Search protein sequence]
THLRPYETLGAHADTMDGVTGTRFSVWAPNARRVSVVGQFNYWDGRRHPM
RLRKESGIWELFIPGAHNGQLYKYEMIDANGNLRLKSDPYAFEAQMRPET
ASLICGLPEKVVQTEERKKANQFDAPISIYEVHLGSWRRHTDNNFWLSYR
ELADQLVPYAKWMGFTHLELLPINEHPFDGSWGYQPTGLYAPTRRFGTRD
DFRYFIDAAHAAGLNVILDWVPGHFPTDDFALAEFDGTNLYEHSTLIYNY
GRREVSNFLVGNALYWIERFGIDALRVDAVASMIYRDYIPNEFGGRENLE
AIEFLRNTNRILGEQVSGAVTMAEESTDFPGVSRPQDMGGLGFWYKWNLG
WMHDTLDYMKLDPVYRQYHHDKLTFGILYNYTENFVLPLSHDEVVHGKKS
ILDRMPGDAWQKFANLRAYYGWMWAFPGKKLLFMGNEFAQGREWNHDASL
DWHLLEGGDNWHHGVQRLVRDLNLTYRHHKAMHELDFDPYGFEWLVVDDK
ERSVLIFVRRDKEGNEIIVASNFTPVPRHDYRFGINQPGKWREILNTDSM
HYHGSNAGNGGTVHSDEIASHGRQHSLSLTLPPLATIWLVREAE
3D structure
PDB5e6y Crystal structures of Escherichia coli branching enzyme in complex with cyclodextrins.
ChainB
Resolution2.6 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 2.4.1.18: 1,4-alpha-glucan branching enzyme.
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 T508 I511 W628 T374 I377 W494
BS02 GLC B T508 F509 T374 F375
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0003844 1,4-alpha-glucan branching enzyme activity
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
GO:0043169 cation binding
Biological Process
GO:0005975 carbohydrate metabolic process
GO:0005978 glycogen biosynthetic process

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Molecular Function
View graph for
Biological Process
External links
PDB RCSB:5e6y, PDBe:5e6y, PDBj:5e6y
PDBsum5e6y
PubMed27139627
UniProtA7ZSW5|GLGB_ECO24 1,4-alpha-glucan branching enzyme GlgB (Gene Name=glgB)

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