Structure of PDB 4lpc Chain C

Receptor sequence
>4lpcC (length=582) Species: 562 (Escherichia coli) [Search protein sequence]
HLRPYETLGAHADTMDGVTGTRFSVWAPNARRVSVVGQFNYWDGRRHPMR
LRKESGIWELFIPGAHNGQLYKYEMIDANGNLRLKSDPYAFEAQMRPETA
SLICGLPEKVVQTEERKKANQFDAPISIYEVHLGSWRRHTDNNFWLSYRE
LADQLVPYAKWMGFTHLELLPINEHPFDGSWGYQPTGLYAPTRRFGTRDD
FRYFIDAAHAAGLNVILDWVPGHFPTDDFALAEFDGTNLYEHSLIYNYGR
REVSNFLVGNALYWIERFGIDALRVDAVASMIYRENLEAIEFLRNTNRIL
GEQVSGAVTMAEESTDFPGVSRPQDMGGLGFWYKWNLGWMHDTLDYMKLD
PVYRQYHHDKLTFGILYNYTENFVLPLSHDEVVHGKKSILDRMPGDAWQK
FANLRAYYGWMWAFPGKKLLFMGNEFAQGREWNHDASLDWHLLEGGDNWH
HGVQRLVRDLNLTYRHHKAMHELDFDPYGFEWLVVDDKERSVLIFVRRDK
EGNEIIVASNFTPVPRHDYRFGINQPGKWREILNTDSMHYHGSNAGNGGT
VHSDEIASHGRQHSLSLTLPPLATIWLVREAE
3D structure
PDB4lpc Crystal Structures of Escherichia coli Branching Enzyme in Complex with Linear Oligosaccharides.
ChainC
Resolution2.39 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 C D542 W544 D396 W398
BS02 GLC C P659 P661 S689 P513 P515 S543
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:4lpc, PDBe:4lpc, PDBj:4lpc
PDBsum4lpc
PubMed26280198
UniProtP07762|GLGB_ECOLI 1,4-alpha-glucan branching enzyme GlgB (Gene Name=glgB)

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