Structure of PDB 5cq1 Chain B

Receptor sequence

>5cq1B (length=511) Species: 3702 (Arabidopsis thaliana)

SVGEDFPSEYEQWLPVPDPESRRRAGVLLHPTSFRGPHGIGDLGEEAFRF
IDWLHSTGCSVWQVLPLVPPDEGGSPYAGQDANCGNTLLISLDELVKDGL
LIKDELPQPIDADSVNYQTANKLKSPLITKAAKRLIDGNGELKSKLLDFR
NDPSISCWLEDAAYFAAIDNTLNAYSWFEWPEPLKNRHLSALEAIYESQK
EFIDLFIAKQFLFQRQWQKVREYARRQGVDIMGDMPIYVGYHSADVWANK
KHFLLNKKGFPLLVSGVPPGQLWGSPLYDWKAMESDQYSWWVNRIRRAQD
LYDECRIDHFRGFAGFWAVPSEAKVAMVGRWKVGPGKSLFDAISKGVGKI
KIIAEDLGVITKDVVELRKSIGAPGMAVLQFAFGGGADNPHLPHNHEVNQ
VVYSGTHDNDTIRGWWDTLDQEEKSKAMKYLSIAGEDDISWSVIQAAFSS
TAQTAIIPMQDILGLGSSARMNTPATEVGNWGWRIPSSTSFDNLETESDR
LRDLLSLYGRL

3D structure

• PDB: 5cq1 Structural Dissection of the Maltodextrin Disproportionation Cycle of the Arabidopsis Plastidial Disproportionating Enzyme 1 (DPE1).
• Chain: B
• Resolution: 2.3 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): D373 E420 D473
• Catalytic site (residue number reindexed from 1): D308 E355 D408
• 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	B	Y136 W338 D373 H472 D473	Y77 W273 D308 H407 D408
BS02	GLC	B	S134 W338 N537 P539 A540	S75 W273 N472 P474 A475
BS03	GLC	B	D373 H374 E420 D473	D308 H309 E355 D408

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:5cq1, PDBe:5cq1, PDBj:5cq1
• PDBsum: 5cq1
• PubMed: 26504082
• UniProt: Q9LV91|DPE1_ARATH 4-alpha-glucanotransferase DPE1, chloroplastic/amyloplastic (Gene Name=DPE1)