Structure of PDB 6s1t Chain B

Receptor sequence
>6s1tB (length=512) Species: 27300 (Schwanniomyces occidentalis) [Search protein sequence]
SIDLSVDTSEYNRPLIHFTPEKGWMNAPNGLFYDKTAKLWHLYFQYNPNA
TAWGQPLYWGHATSNDLVHWDEHEIAIGPEHDNEGIFSGSIVVDHNNTSG
FFNSSIDPNQRIVAIYTNNIPDNQTQDIAFSLDGGYTFTKYENNPVIDVS
SNQFRDPKVFWHEDSNQWIMVVSKSQEYKIQIFGSANLKNWVLNSNFSSG
YYGNQYECPGLIEVPIENSDKSKWVMFLAINPGSPLGGSINQYFVGDFDG
FQFVPDDSQTRFVDIGKDFYAFQTFSEVEHGVLGLAWASNWQYADQVPTN
PWRSSTSLARNYTLRYVHTNAETKQLTLIQNPVLPDSINVVDKLKKKNVK
LTNKKPIKTNFKGSTGLFDFNITFKVLNLNVSPGKTHFDILINSQELNSS
VDSIKIGFDSSQSSFYIDRHIPNVEFPRKQFFTDKLAAYLEPLDYDQDLR
VFSLYGIVDKNIIELYFNDGTVAMTNTFFMGEGKYPHDIQIVTDTEEPLF
ELESVIIRELNK
3D structure
PDB6s1t New insights into the molecular mechanism behind mannitol and erythritol fructosylation by beta-fructofuranosidase from Schwanniomyces occidentalis.
ChainB
Resolution2.09 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) A50 E230
Catalytic site (residue number reindexed from 1) A27 E207
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 GLC B W76 E230 W314 W53 E207 W291
BS02 FRU B N49 Q68 S111 R178 D179 E230 Y293 W314 N26 Q45 S88 R155 D156 E207 Y270 W291
Gene Ontology
Molecular Function
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
Biological Process
GO:0005975 carbohydrate metabolic process

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:6s1t, PDBe:6s1t, PDBj:6s1t
PDBsum6s1t
PubMed33785821
UniProtE5D0X5

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