Structure of PDB 5cpt Chain A

Receptor sequence
>5cptA (length=514) Species: 3702 (Arabidopsis thaliana) [Search protein sequence]
SVGEDFPSEYEQWLPVPDPESRRRAGVLLHPTSFRGPHGIGDLGEEAFRF
IDWLHSTGCSVWQVLPLVPPDEGGSPYAGQDANCGNTLLISLDELVKDGL
LIKDELPQPIDADSVNYQTANKLKSPLITKAAKRLIDGNGELKSKLLDFR
NDPSISCWLEDAAYFAAIDNTLNAYSWFEWPEPLKNRHLSALEAIYESQK
EFIDLFIAKQFLFQRQWQKVREYARRQGVDIMGDMPIYVGYHSADVWANK
KHFLLNKKGFPLLVSGVPPSETGQLWGSPLYDWKAMESDQYSWWVNRIRR
AQDLYDECRIDHFRGFAGFWAVPSEAKVAMVGRWKVGPGKSLFDAISKGV
GKIKIIAEDLGVITKDVVELRKSIGAPGMAVLQFAFGGGADNPHLPHNHE
VNQVVYSGTHDNDTIRGWWDTLDQEEKSKAMKYLSIAGEDDISWSVIQAA
FSSTAQTAIIPMQDILGLGSSARMNTPATEVGNWGWRIPSSTSFDNLETE
SDRLRDLLSLYGRL
3D structure
PDB5cpt Structural Dissection of the Maltodextrin Disproportionation Cycle of the Arabidopsis Plastidial Disproportionating Enzyme 1 (DPE1).
ChainA
Resolution2.3 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D373 E420 D473
Catalytic site (residue number reindexed from 1) D311 E358 D411
Enzyme Commision number 2.4.1.25: 4-alpha-glucanotransferase.
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 BGC A Y136 D373 H472 D473 Y77 D311 H410 D411
BS02 GLC A S134 A137 N537 P539 A540 S75 A78 N475 P477 A478
Gene Ontology
Molecular Function
GO:0004134 4-alpha-glucanotransferase activity
GO:0016757 glycosyltransferase activity
Biological Process
GO:0000025 maltose catabolic process
GO:0005975 carbohydrate metabolic process
GO:0005983 starch catabolic process
GO:0006006 glucose metabolic process
Cellular Component
GO:0009501 amyloplast
GO:0009507 chloroplast

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:5cpt, PDBe:5cpt, PDBj:5cpt
PDBsum5cpt
PubMed26504082
UniProtQ9LV91|DPE1_ARATH 4-alpha-glucanotransferase DPE1, chloroplastic/amyloplastic (Gene Name=DPE1)

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