Structure of PDB 6y9t Chain A

Receptor sequence
>6y9tA (length=536) Species: 272621 (Lactobacillus acidophilus NCFM) [Search protein sequence]
MSHWYDHAIIYQIYPKSFQDSNDDGIGDLNGIRKRIPYLQNLGVNAVWLN
PVFVSPQVDNGYDVSNYFAIDSHMGTMEDMENLIKDLHKAGIHIIMDFVL
NHTSDQHPWFQDAIKNPDSLYRDYYIFAGHDNKQPNNWGSFFGGSVWEPD
PAGTGQSYFHLFDKRMPDLNWKNPEVRHAMLEIAEFWLKKGIDGLRLDAF
IHIGKADLRQNYPAMDDKPVIAEPFFANLPQVQEWMRPFCEQIKEDYPDA
LLLGEAASASVNLAVDYTNKRNHLMDCVITFRYFTSAQYQPKELDLTAFK
QNQVVWQQTLADISQPTLYWNNHDMARLATRIAKTSTQAKSLAMLMYLQR
GIPIIYYGEELGLKNLHFTSVDQFEDQTVAPWIKEAQKAGISRDAAFAMV
SDTHKLPARGPMPWNDTENNGFTSAKPWLNGISQDDVTVANEVNSDNSMF
TFYKNMLNLKKEKLFQDGTYYMISTGKDSYVYQRDLGNESAIVAVSLSNK
KISIDLPEELLKAGEYQLTNGKLTLMPYAGVVLKKE
3D structure
PDB6y9t An 1,4-alpha-Glucosyltransferase Defines a New Maltodextrin Catabolism Scheme in Lactobacillus acidophilus.
ChainA
Resolution2.78 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D97 R196 D198 E255 H333 D334
Catalytic site (residue number reindexed from 1) D97 R196 D198 E255 H323 D324
Enzyme Commision number 3.2.1.10: oligo-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 CA A D20 N22 D24 I26 D28 D20 N22 D24 I26 D28
Gene Ontology
Molecular Function
GO:0004556 alpha-amylase activity
GO:0004574 oligo-1,6-glucosidase activity
GO:0016798 hydrolase activity, acting on glycosyl bonds
GO:0046872 metal ion binding
Biological Process
GO:0005975 carbohydrate metabolic process
GO:0009313 oligosaccharide catabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:6y9t, PDBe:6y9t, PDBj:6y9t
PDBsum6y9t
PubMed32444471
UniProtQ5FI02

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