Structure of PDB 7c27 Chain A

Receptor sequence
>7c27A (length=372) Species: 479435 (Kribbella flavida DSM 17836) [Search protein sequence]
GLDSHELARLHELARHSHAVITRHQDAGGAYPAAPTFSAYRGYAWLRDGS
FTAEGISRYGDVASAGRFHDWVDGVLRRRRGQVDDLLAAVDRGEVPSNEG
MLPTRFTFDGNDGSDPWWDFQTDGYGMWLWSVVTHAARHGLDLERWRAGI
DVAVDYLLAFWDRPCYDWWEEHVEHRHVSTLGAIHGGLVAVGTCAALRSA
PWSAATLQVAARIRSLVSAEGVVDGHLVKWLGSSAVDGSLPACVVPFGLV
PPDDDVAAMTRAAVAKDLDVDGGVHRFAADVYYGGGQWILLSALLGWNLA
AAGDTAGALRHLRWIADQADADGDLPEQVPHHLLHPGSRAEWVARWGTVA
TPLLWSHGMYLILADELGLLPP
3D structure
PDB7c27 Structural insights reveal the second base catalyst of isomaltose glucohydrolase.
ChainA
Resolution1.91 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 3.2.1.205: isomaltose glucohydrolase.
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 GOL A Y48 R55 D56 Y40 R47 D48
BS02 GOL A W177 R284 W169 R276
BS03 GOL A R222 S226 L257 R214 S218 L249
Gene Ontology
Molecular Function
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
GO:0016798 hydrolase activity, acting on glycosyl bonds
Biological Process
GO:0000272 polysaccharide catabolic process
GO:0005975 carbohydrate metabolic process
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:7c27, PDBe:7c27, PDBj:7c27
PDBsum7c27
PubMed34665923
UniProtD2PPM8|IMGH_KRIFD Isomaltose glucohydrolase (Gene Name=Kfla_1896)

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