Structure of PDB 6r3u Chain A

Receptor sequence
>6r3uA (length=495) Species: 818 (Bacteroides thetaiotaomicron) [Search protein sequence]
DGTATYFQSSDEHGFSMYYKPQVGFVGDPMPFYDPVAKDFKVMYLQDYRP
NPEATYHPIFGVATKDGATYESLGELISCGGRDEQDAAIGTGGTIYNPAD
KLYYTFYTGNKFKPSSDQNAQVVMVATSPDFKTWTKNRTFYLKGDTYGYD
KNDFRDPFLFQTEDGVYHMLIATRKNGKGHIAEFTSADLKEWESAGTFMT
MMWDRFYACPDVFKMGDWWYLIYSEQASFMRKVQYFKGRTLEDLKATTAN
DAGIWPDNREGMLDSRAFYAGKTASDGTNRYIWGWCPTRAGNDNGNVGDV
EPEWAGNLVAQRLIQHEDGTLTLGVPDAIDRKYTSAQEVKVMAKDGNMIE
SGKTYTLGEGASVIFNRLKVHNKISFTVKTASNTDRFGISFVRGTDSASW
YSIHVNADEGKANFEKDGDDAKYLFDNKFNIPADNEYRVTIYSDQSVCVT
YINDQLSFTNRIYQMQKNPWSLCCYKGEITVSDVQVSTYHHHHHH
3D structure
PDB6r3u First crystal structure of an endo-levanase - the BT1760 from a human gut commensal Bacteroides thetaiotaomicron.
ChainA
Resolution1.9 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 3.2.1.26: beta-fructofuranosidase.
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 FRU A R244 E314 R231 E301
BS02 FRU A D41 T104 R168 D169 W317 D28 T91 R155 D156 W304
BS03 FRU A H70 I102 H57 I89
BS04 FRU A N64 Y69 H70 W317 N51 Y56 H57 W304
BS05 ZN A H26 H384 H503 H13 H371 H490
Gene Ontology
Molecular Function
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
GO:0016798 hydrolase activity, acting on glycosyl bonds
GO:0046872 metal ion binding
Biological Process
GO:0005975 carbohydrate metabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:6r3u, PDBe:6r3u, PDBj:6r3u
PDBsum6r3u
PubMed31186460
UniProtQ8A6W6

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