Structure of PDB 5cps Chain B

Receptor sequence

>5cpsB (length=512) Species: 3702 (Arabidopsis thaliana)

SVGEDFPSEYEQWLPVPDPESRRRAGVLLHPTSFRGPHGIGDLGEEAFRF
IDWLHSTGCSVWQVLPLVPPDEGGSPYAGQDANCGNTLLISLDELVKDGL
LIKDELPQPIDADSVNYQTANKLKSPLITKAAKRLIDGNGELKSKLLDFR
NDPSISCWLEDAAYFAAIDNTLNAYSWFEWPEPLKNRHLSALEAIYESQK
EFIDLFIAKQFLFQRQWQKVREYARRQGVDIMGDMPIYVGYHSADVWANK
KHFLLNKKGFPLLVSGVPPTGQLWGSPLYDWKAMESDQYSWWVNRIRRAQ
DLYDECRIDHFRGFAGFWAVPSEAKVAMVGRWKVGPGKSLFDAISKGVGK
IKIIAEDLGVITKDVVELRKSIGAPGMAVLQFAFGGGADNPHLPHNHEVN
QVVYSGTHDNDTIRGWWDTLDQEEKSKAMKYLSIAGEDDISWSVIQAAFS
STAQTAIIPMQDILGLGSSARMNTPATEVGNWGWRIPSSTSFDNLETESD
RLRDLLSLYGRL

3D structure

• PDB: 5cps Structural Dissection of the Maltodextrin Disproportionation Cycle of the Arabidopsis Plastidial Disproportionating Enzyme 1 (DPE1).
• Chain: B
• Resolution: 1.8 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): D373 E420 D473
• Catalytic site (residue number reindexed from 1): D309 E356 D409
• 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	GLC	B	G423 H456	G359 H392
BS02	GLC	B	Q336 W338 H374 E420	Q272 W274 H310 E356
BS03	GLC	B	Y136 H472 D473	Y77 H408 D409
BS04	GLC	B	S134 N537 A540	S75 N473 A476
BS05	GLC	B	D130 E542	D71 E478

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

External links

• PDB: RCSB:5cps, PDBe:5cps, PDBj:5cps
• PDBsum: 5cps
• PubMed: 26504082
• UniProt: Q9LV91|DPE1_ARATH 4-alpha-glucanotransferase DPE1, chloroplastic/amyloplastic (Gene Name=DPE1)