Structure of PDB 7ejt Chain B

Receptor sequence
>7ejtB (length=1526) Species: 284593 (Nakaseomyces glabratus CBS 138) [Search protein sequence]
AHRTLLLRLSDSGEPVTSCSYGQGVLTLPSLPLPQGKKLGDMPVYTVKLA
IPAGSPVTRDGLIWTNCPPDFSTQFDREKFYKKIIKTSFHEDDHIDLDIY
VPGTYCFYLSFKNDKDELETTRKFYFVVLPILSVNDKFIPLNSIAMQSVV
SKWMGPTIKDWEKVFARVASKKYNMIHFTPLQHRGESNSPYSIYDQLEFD
PTVFKSEKEVADMVERLRTEHNILSLTDIVFNHTANNSQWLLDHPEAGYN
HKTSPHLISAIELDKKLLDFSEQMEALGYPVDLKTVDDLIKVMDGIKEHV
IGELKLWEFYVVDVKQTVSELREKWGNSKSWSDDNIPSKDDSTNLAQFVR
DNATEPGFGSLGERGSNKINIDKFAAILKKLHSEDYNNGIEELATKILND
INLPFYKEYDDDINEVLEQLFNRIKYLRIDDHGPKQGPITKKLPLSEPYF
TRFKAKDGEEYALANNGAIWDGNPLVDFASSQSKAYLRREVIVWGDCVKL
RYGKGPSDSPYLWERMSKYVEMNARIFNGFRIDNCHSTPLHVGQYFLDVA
RRVNPNLYVVAELFSGSEAMDCLFVERLGISSLIREAMQAWSEEELSRLV
HRHGGRPIGSYKFVPLDDFPYPADVKIDEEYCAYNPDDHSVKCVSEIMIP
KTLTATPPHALFMDCTHDNETPNQKRTVEDTLPNAALVAFCSSAIGSVYG
YDEVFPQLLDLVQEKRTYSCAENTGISKVKTLLNNMREEIASEAVDIEDS
EMHVHHDGQYITFHRTNAKNGKGWYLVARTKFHSSGDQMLPRIKLSQTKA
TFKAAFSLERTGDAPISDEIIEGIPTKLRELTGFDIGFDENTKETSILLP
QDFPQGSIVIFETQQLGIDDSLDHFIRSGAIKATEKLSLESINYVLYRAE
QEEYDYSEGRSGAYDIPDYGKPVYCGLQGWVSILRKIIFYNDLAHPLSNN
LRNGHWAVDYVVNRLDLYKDKEGVAEVQEWLRSRMERIKQLPSYLVPSFF
ALVVGIMYGCCRLRAMQLMSDNVGKSTVFVQSLAMTSIQMVSAMKSTSIL
PDQNIAAMAAGLPHFSTNYMRCWGRDVFISLRGLLLTTGRYEEAKEHILA
FAKTLKHGLIPNLLDAGRNPRYNARDAAWFFVQAIQDYVTIVPGGVSLLQ
EKVTRRFPLDDEYIPYDDPKAFSYSSTIEEIIYEILNRHAGGIKYREANA
GPNLDRVMKDEGFNVEVNVDWETGLIHGGSQFNCGTWMDKMGESEKANSV
GVPGTPRDGAAVEINGLLKSCLRFVLQLSKDGKFKYTEVTKPDGSKISLS
SWNDLLQENFERCFYVPKNKEDDNKFEIDATIINRRGIYKDLYRSGKPYE
DYQFRPNFTIAMVVAPELFTPDYAAGAIELADQVLRGPVGMRTLDPSDYN
YRPYYNNGEDSDDFATSKGRNYHQGPEWVWCYGYFIRAYHYFNFLTNPKC
QVEGSAKKLKPSSYLYRKLYSRLLKHREWIENSPWAGLAELTNKDGEVCN
DSSPTQAWSTGCLLDLFYDLWISYEE
3D structure
PDB7ejt Crystal structures of glycogen-debranching enzyme mutants in complex with oligosaccharides.
ChainB
Resolution3.2 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 2.4.1.25: 4-alpha-glucanotransferase.
3.2.1.33: amylo-alpha-1,6-glucosidase.
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 I1335 N1336 Y1401 I1333 N1334 Y1399
BS02 GLC B Y916 D917 W958 Y914 D915 W956
BS03 GLC B H1066 N1409 H1064 N1407
BS04 GLC B K1242 Y1407 N1409 Y1424 K1240 Y1405 N1407 Y1422
BS05 GLC B D1241 M1243 D1239 M1241
BS06 GLC B R1123 L1206 D1207 R1121 L1204 D1205
Gene Ontology
Molecular Function
GO:0004134 4-alpha-glucanotransferase activity
GO:0004135 amylo-alpha-1,6-glucosidase activity
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
GO:0016757 glycosyltransferase activity
GO:0016798 hydrolase activity, acting on glycosyl bonds
Biological Process
GO:0005975 carbohydrate metabolic process
GO:0005978 glycogen biosynthetic process
GO:0005980 glycogen catabolic process
Cellular Component
GO:0005575 cellular_component
GO:0005737 cytoplasm

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:7ejt, PDBe:7ejt, PDBj:7ejt
PDBsum7ejt
PubMed34726181
UniProtQ6FSK0

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