Structure of PDB 3vu2 Chain B

Receptor sequence
>3vu2B (length=691) Species: 39947 (Oryza sativa Japonica Group) [Search protein sequence]
DHLPIYDLDPKLEEFKDHFNYRIKRYLDQKCLIEKHEGGLEEFSKGYLKF
GINTVDGATIYREWAPAAQEAQLIGEFNNWNGAKHKMEKDKFGIWSIKIS
HVNGKPAIPHNSKVKFRFRHGGGAWVDRIPAWIRYATFDASKFGAPYDGV
HWDPPACERYVFKHPRPPKPDAPRIYEAHVGMSGEEPEVSTYREFADNVL
PRIRANNYNTVQLMAIMEHSYYASFGYHVTNFFAVSSRSGTPEDLKYLVD
KAHSLGLRVLMDVVHSHASNNVTDGLNGYDVGQNTHESYFHTGDRGYHKL
WDSRLFNYANWEVLRFLLSNLRYWMDEFMFDGFRFDGVTSMLYHHHGINK
GFTGNYKEYFSLDTDVDAIVYMMLANHLMHKLLPEATIVAQDVSGMPVLC
RPVDEGGVGFDFRLAMAIPDRWIDYLKNKEDRKWSMSEIVQTLTNRRYTE
KCIAYAESHDQSIVGDKTIAFLLMDKEMYTGMSDLQPASPTINRGIALQK
MIHFITMALGGDGYLNFMGNEFGHPEWIDFPREGNNWSYDKCRRQWSLVD
TDHLRYKYMNAFDQAMNALEEEFSFLSSSKQIVSDMNEKDKVIVFERGDL
VFVFNFHPNKTYKGYKVGCDLPGKYRVALDSDALVFGGHGRVGHDVDHFT
SPEGMPGVPETNFNNRPNSFKVLSPPRTCVAYYRVDEDREE
3D structure
PDB3vu2 Crystal structure of the rice branching enzyme I (BEI) in complex with maltopentaose.
ChainB
Resolution2.23 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 W72 P74 F100 H294 E295 W64 P66 F92 H286 E287
BS02 GLC B F100 W319 E320 F92 W311 E312
BS03 GLC B H44 E45 F100 H36 E37 F92
BS04 BGC B K123 D135 K115 D127
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
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Biological Process
External links
PDB RCSB:3vu2, PDBe:3vu2, PDBj:3vu2
PDBsum3vu2
PubMed22771800
UniProtQ01401|GLGB_ORYSJ 1,4-alpha-glucan-branching enzyme, chloroplastic/amyloplastic (Gene Name=SBE1)

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