Structure of PDB 7ejp Chain A

Receptor sequence
>7ejpA (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
PDB7ejp Crystal structures of glycogen-debranching enzyme mutants in complex with oligosaccharides.
ChainA
Resolution3.1 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 A Y1351 D1400 Y1401 Y1349 D1398 Y1399
BS02 GLC A Y916 D917 W958 Y914 D915 W956
BS03 GLC A H1066 M1072 D1503 H1064 M1070 D1501
BS04 GLC A K1242 Y1407 N1409 Y1424 K1240 Y1405 N1407 Y1422
BS05 GLC A W1075 D1241 K1242 M1243 W1073 D1239 K1240 M1241
BS06 GLC A L1206 D1207 L1204 D1205
BS07 GLC A Y1071 L1206 Y1069 L1204
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:7ejp, PDBe:7ejp, PDBj:7ejp
PDBsum7ejp
PubMed34726181
UniProtQ6FSK0

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