Structure of PDB 1jak Chain A

Receptor sequence
>1jakA (length=499) Species: 1922 (Streptomyces plicatus) [Search protein sequence]
DRKAPVRPTPLDRVIPAPASVDPGGAPYRITRGTHIRVDDSREARRVGDY
LADLLRPATGYRLPVTAHGHGGIRLRLAGGPYGDEGYRLDSGPAGVTITA
RKAAGLFHGVQTLRQLLPPAVEKDSAQPGPWLVAGGTIEDTPRYAWRSAM
LDVSRHFFGVDEVKRYIDRVARYKYNKLHLHLSDDQGWRIAIDSWPRLAT
YGGSTEVGGGPGGYYTKAEYKEIVRYAASRHLEVVPEIDMPGHTNAALAS
YAELNCDGVAPPLYTGTKVGFSSLCVDKDVTYDFVDDVIGELAALTPGRY
LHIGGDEAHSTPKADFVAFMKRVQPIVAKYGKTVVGWHQLAGAEPVEGAL
VQYWGLDRTGDAEKAEVAEAARNGTGLILSPADRTYLDMKYTKDTPLGLS
WAGYVEVQRSYDWDPAGYLPGAPADAVRGVEAPLWTETLSDPDQLDYMAF
PRLPGVAELGWSPASTHDWDTYKVRLAAQAPYWEAAGIDFYRSPQVPWT
3D structure
PDB1jak Biochemical and structural assessment of the 1-N-azasugar GalNAc-isofagomine as a potent family 20 beta-N-acetylhexosaminidase inhibitor.
ChainA
Resolution1.75 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) D313 E314
Catalytic site (residue number reindexed from 1) D306 E307
Enzyme Commision number 3.2.1.52: beta-N-acetylhexosaminidase.
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 CL A D175 R176 R179 D168 R169 R172
BS02 IFG A R162 D313 E314 W344 W361 Y393 D395 W408 W442 E444 R155 D306 E307 W337 W354 Y386 D388 W401 W435 E437 MOAD: Ki=2.7uM
PDBbind-CN: -logKd/Ki=5.57,Ki=2.7uM
Gene Ontology
Molecular Function
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
GO:0004563 beta-N-acetylhexosaminidase activity
GO:0016787 hydrolase activity
Biological Process
GO:0005975 carbohydrate metabolic process
GO:0030203 glycosaminoglycan metabolic process
Cellular Component
GO:0016020 membrane

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:1jak, PDBe:1jak, PDBj:1jak
PDBsum1jak
PubMed11522797
UniProtO85361

[Back to BioLiP]