Structure of PDB 5dkz Chain A

Receptor sequence
>5dkzA (length=921) Species: 759272 (Thermochaetoides thermophila DSM 1495) [Search protein sequence]
EHDWKKCDQSGFCRRNRAYADHALSAISWESPYKIAPETGSFKDGQYQAI
ILKTINDHGETVRLPLTVSFLESGTARVTIDEEKRQKGEIELRHDSKARK
ERYNEAEQWVIVGGMTLDKGAKVDYEDKTQMTVKYGPSSKFEATIKFAPF
SIDFKRDGASHIKFNDQGLLNIEHWRPKIDPPDDSTWWEESFGGNTDSKP
RGPESVGLDISFVGYEHVFGIPSHASPLSLKQTRGGEGNYNEPYRMYNAD
VFEYILDSPMTLYGSIPFMQAHRKDSSVGIFWLNAAETWVDITKGKDSKN
PLALGVKSKITTRTHWFSESGLLDVFVFLGPTPKDIISKYAELTGTTAMP
QEFSLGYHQCRWNYVSDEDVKDVDRKMDKFNMPYDVIWLDIEYTDEKKYF
TWDKHSFKDPIGMGKQLEAHGRKLVTIIDPHIKNTNNYPVVDELKSKDLA
VKTKDGSIFEGWCWPGSSHWIDAFNPAAREWWKGLFKYDKFKGTMENTFI
WNAMNEPSVFNGPEVTMPKDNLHHGNWEHRDVHNLNGMTFQNATYHALLS
RKPGEHRRPFVLTRAFFAGSQRLGAMWTGDNTADWGYLKASIPMVLSQGI
AGFPFAGADVGGFFGNPDKDLLTRWYQTGIFYPFFRAHAHIDARRREPYL
TGEPYNTIIAAALRLRYSLLPSWYTAFRHAHLDGTPIIKPMFYTHPSEEA
GLPIDDQFFIGNTGLLAKPVTDKDRTSVDIWIPDSEVYYDYFTYDIISAA
KSKTATLDAPLEKIPLLMRGGHVFARRDIPRRSSALMKWDPYTLVVVLGN
DRKAEGDLYVDDGDSFDYEKGQYIHRRFIFDANTLTSADYEGRDDKEGEW
LKKMRTVNVEKIIVVGAPAAWKGKKTVTVESEGKTWAAAIEYNPAEKSRA
AFAVVKKVGVRVGADFKIVFG
3D structure
PDB5dkz Structural basis for two-step glucose trimming by glucosidase II involved in ER glycoprotein quality control.
ChainA
Resolution2.4 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 3.2.1.20: alpha-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 D303 W415 M557 D633 F666 D250 W362 M504 D580 F613
BS02 GLC A D443 R617 W630 D633 F666 H691 D390 R564 W577 D580 F613 H638
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
GO:0016798 hydrolase activity, acting on glycosyl bonds
GO:0030246 carbohydrate binding
GO:0090599 alpha-glucosidase activity
Biological Process
GO:0005975 carbohydrate metabolic process
GO:0006491 N-glycan processing
Cellular Component
GO:0017177 glucosidase II complex

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:5dkz, PDBe:5dkz, PDBj:5dkz
PDBsum5dkz
PubMed26847925
UniProtG0SG42

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