Structure of PDB 5ohs Chain D

Receptor sequence
>5ohsD (length=662) Species: 358 (Agrobacterium tumefaciens) [Search protein sequence]
MHFETTKDGFTIAIGNRIILSHSPDKPAFFAGFGEERMDMYRGNFDIEDY
VIERTALRHAEVSGDSVTLSSAPGQAPRLRLTLDGNAIRLTALDETINRL
WLRVVAETDEHVWGGGEQMSYFDMRGRRFPLWTSEPGVGRDKTTEITFKS
DVSGKAGGDYYNTNYPQPTWLSSRKYALHVETSAYSVFDFRNGDFHEIEI
WAVPEKIEFFAGDSFADIVSALSLHFGRQPELPDWVYNGAIIGLKDGVNS
FARLEKIRAAGTKVSGLWCEDWVGLRQTSFGARLFWDWQANDTRYPHLRQ
KIAELADQGIRFLGYVNPYLCVDGPLFPVAESAGYFATDVDGKTALVDFG
EFDCGVVDFTNPAAADWFAAAIIGKNMLDFGLSGWMADFGEYLPIDIKLS
NGVDAKLMHNAWPTLWAEVNAKGVESRGKTGEALFFMRAGFTGVQAHCPL
IWGGNQSVDFSRHDGLVTVICGALSSGLMGNAYHHSDIGGYTSLFGNVRT
AELIMRWTEMAAFTPVMRTHEGNRPRDNLQIDQDETVLAHFARMTAIYVA
LAPYLKSLSAEAAKTGLPVQRPLFLHYENEPQTYAVQDCYLYGADMLVAP
VWKAGETQRSLYLPGHGEWVHLWSGKRHAGGRDITVETPLGEPAVFYRAD
SSHHRLFEQLRT
3D structure
PDB5ohs Structural and Biochemical Insights into the Function and Evolution of Sulfoquinovosidases.
ChainD
Resolution1.97 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 3.2.1.-
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 NSQ D E270 R283 L284 W286 M386 D388 R438 N455 Y491 H520 E270 R283 L284 W286 M386 D388 R438 N455 Y491 H520
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
Biological Process
GO:0005975 carbohydrate metabolic process

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Molecular Function
View graph for
Biological Process
External links
PDB RCSB:5ohs, PDBe:5ohs, PDBj:5ohs
PDBsum5ohs
PubMed30276262
UniProtA9CEZ0|SQASE_AGRFC Sulfoquinovosidase (Gene Name=smoI)

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