Structure of PDB 5oht Chain B

Receptor sequence
>5ohtB (length=666) Species: 83333 (Escherichia coli K-12) [Search protein sequence]
LDFQFHQNDSFTLHFQQRLILTHSKDNPCLWIGSGIADIDMFRGNFSIKD
KLQEKIALTDAIVSQSPDGWLIHFSRGSDISATLNISADRLLLELQNDNL
NHNRIWLRLAAQPEDHIYGCGEQFSYFDLRGKPFPLWTSEQGVGRNKQTY
VTWQADCKENAGGDYYWTFFPQPTFVSTQKYYCHVDNSCYMNFDFSAPEY
HELALWEDKATLRFECADTYISLLEKLTALLGRQPELPDWIYDGVTLGIQ
GGTEVCQKKLDTMRNAGVKVNGIWAQDWSGIRMTSFGKRVMWNWKWNSEN
YPQLDSRIKQWNQEGVQFLAYINPYVASDKDLCEEAAQHGYLAKDASGGD
YLVEFGEFYGGVVDLTNPEAYAWFKEVIKKNMIELGCGGWMADFGEYLPT
DTYLHNGVSAEIMHNAWPALWAKCNYEALEETGKLGEILFFMRAGSTGSQ
KYSTMMWAGDQNVDWSLDDGLASVVPAALSLAMTGHGLHHSDIGGYTTLF
EMKRSKELLLRWCDFSAFTPMMRTHEGNRPGDNWQFDGDAETIAHFARMT
TVFTTLKPYLKEAVALNAKSGLPVMRPLFLHYEDDAHTYTLKYQYLLGRD
ILVAPVHEEGRSDWTLYLPEDNWVHAWTGEAFRGGEVTVNAPIGKPPVFY
RADSEWAALFASLKSI
3D structure
PDB5oht Structural and Biochemical Insights into the Function and Evolution of Sulfoquinovosidases.
ChainB
Resolution1.87 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 3.2.1.199: sulfoquinovosidase.
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 B Q153 G154 D472 D481 Q141 G142 D460 D469
BS02 9VH B Q288 R301 V302 W304 M403 D405 Y508 H537 Q276 R289 V290 W292 M391 D393 Y496 H525
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:1990929 sulfoquinovosidase activity
Biological Process
GO:0005975 carbohydrate metabolic process
GO:0061720 6-sulfoquinovose(1-) catabolic process to glycerone phosphate and 3-sulfolactaldehyde

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Molecular Function
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Biological Process
External links
PDB RCSB:5oht, PDBe:5oht, PDBj:5oht
PDBsum5oht
PubMed30276262
UniProtP32138|SQASE_ECOLI Sulfoquinovosidase (Gene Name=yihQ)

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