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BioLiP

Structure of PDB 6lx1 Chain A

Receptor sequence
>6lx1A (length=515) Species: 4113 (Solanum tuberosum) [Search protein sequence]
VPAVGEDFPIDYADWLPKRDPNDRRRAGILLHPTSFPGPYGIGDLGPQAF
KFLDWLHLAGCSLWQVLPLVPPGKRGDGSPYSGQDANCGNTLLISLEELV
DDGLLKMEELPEPLPTDRVNYSTISEIKDPLITKAAKRLLSSEGELKDQL
ENFRRDPNISSWLEDAAYFAAIDNSVNTISWYDWPEPLKNRHLAALEEVY
QSEKDFIDIFIAQQFLFQRQWKKVRDYARSKGISIMGDMPIYVGYHSADV
WANKKQFLLNRKGFPLIVSGVPPGQLWGSPLYDWKAMEKDGFSWWVRRIQ
RATDLFDEFRIDHFRGFAGFWAVPSEEKIAILGRWKVGPGKPLFDAILQA
VGKINIIAEDLGVITEDVVQLRKSIEAPGMAVLQFAFGSDAENPHLPHNH
EQNQVVYTGTHDNDTIRGWWDTLPQEEKSNVLKYLSNIEEEEISRGLIEG
AVSSVARIAIIPMQDVLGLGSDSRMNIPATQFGNWSWRIPSSTSFDNLDA
EAKKLRDILATYGRL
3D structure
PDB6lx1 Structural analysis and reaction mechanism of the disproportionating enzyme (D-enzyme) from potato.
ChainA
Resolution2.03 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D321 E368 D421
Catalytic site (residue number reindexed from 1) D312 E359 D412
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 ASO A Y84 D321 H420 D421 Y81 D312 H411 D412
BS02 AC1 A S85 N485 A488 Q490 S82 N476 A479 Q481
BS03 MG A E189 H195 E186 H192
Gene Ontology
Molecular Function
GO:0004134 4-alpha-glucanotransferase activity
GO:0016757 glycosyltransferase activity
Biological Process
GO:0005975 carbohydrate 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:6lx1, PDBe:6lx1, PDBj:6lx1
PDBsum6lx1
PubMed32808707
UniProtQ06801|DPEP_SOLTU 4-alpha-glucanotransferase, chloroplastic/amyloplastic (Gene Name=DPEP)

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