Structure of PDB 2w4x Chain A Binding Site BS01

Receptor Information
>2w4x Chain A (length=579) Species: 226186 (Bacteroides thetaiotaomicron VPI-5482) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
SLQPPPQQLIVQNKTIDLPAVYQLNGGEEANPHAVKVLKELLSGMLISIG
EKGDKSVRKYSRQIPDHKEGYYLSVNEKEIVLAGNDERGTYYALQTFAQL
LKDGKLPEVEIKDYPSVRYRGVVEGFYGTPWSHQARLSQLKFYGKNKMNT
YIYGPKDDPYHSAPNWRLPYPDKEAAQLQELVAVANENEVDFVWAIHPGQ
DIKWNKEDRDLLLAKFEKMYQLGVRSFAVFFDDISGEGTNPQKQAELLNY
IDEKFAQVKPDINQLVMCPTEYNKSWSNPNGNYLTTLGDKLNPSIQIMWT
GDRVISDITRDGISWINERIKRPAYIWWNFPVSDYVRDHLLLGPVYGNDT
TIAKEMSGFVTNPMEHAESSKIAIYSVASYAWNPAKYDTWQTWKDAIRTI
LPSAAEELECFAMHNSDLGPNGHGYRREESMDIQPAAERFLKAFKEGKNY
DKADFETLQYTFERMKESADILLMNTENKPLIVEITPWVHQFKLTAEMGE
EVLKMVEGRNESYFLRKYNHVKALQQQMFYIDQTSNQNPYQPGVKTATRV
IKPLIDRTFATVVKFFNQKFNAHLDATTD
Ligand information
Ligand IDSTZ
InChIInChI=1S/C8H15N3O7/c1-11(10-17)8(16)9-4-6(14)5(13)3(2-12)18-7(4)15/h3-7,12-15H,2H2,1H3,(H,9,16)/t3-,4-,5-,6-,7-/m1/s1
InChIKeyZSJLQEPLLKMAKR-NYMZXIIRSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.6.1CN(C(=O)N[C@@H]1[C@H]([C@@H]([C@H](O[C@H]1O)CO)O)O)N=O
OpenEye OEToolkits 1.6.1CN(C(=O)NC1C(C(C(OC1O)CO)O)O)N=O
CACTVS 3.352CN(N=O)C(=O)N[C@H]1[C@H](O)O[C@H](CO)[C@@H](O)[C@@H]1O
CACTVS 3.352CN(N=O)C(=O)N[CH]1[CH](O)O[CH](CO)[CH](O)[CH]1O
ACDLabs 10.04O=NN(C(=O)NC1C(O)C(O)C(OC1O)CO)C
FormulaC8 H15 N3 O7
NameStreptozotocin;
2-deoxy-2-{[methyl(nitroso)carbamoyl]amino}-beta-D-glucopyranose
ChEMBL
DrugBank
ZINCZINC000003995968
PDB chain2w4x Chain A Residue 1591 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB2w4x Structural Insight Into the Mechanism of Streptozotocin Inhibition of O-Glcnacase.
Resolution2.42 Å
Binding residue
(original residue number in PDB)		G135 D242 Y282 V314 W337 D344 Y345
Binding residue
(residue number reindexed from 1)		G125 D232 Y272 V304 W327 D334 Y335
Annotation score2
Binding affinityMOAD: Kd=14uM
PDBbind-CN: -logKd/Ki=4.85,Kd=14uM
Enzymatic activity
Enzyme Commision number 3.2.1.169: protein O-GlcNAcase.
Gene Ontology
Molecular Function
GO:0015929 hexosaminidase activity
GO:0016231 beta-N-acetylglucosaminidase activity
GO:0016798 hydrolase activity, acting on glycosyl bonds
GO:0042802 identical protein binding
GO:0102571 [protein]-3-O-(N-acetyl-D-glucosaminyl)-L-serine/L-threonine O-N-acetyl-alpha-D-glucosaminase activity
Biological Process
GO:0005975 carbohydrate metabolic process
GO:0006517 protein deglycosylation
GO:1901135 carbohydrate derivative metabolic process

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:2w4x, PDBe:2w4x, PDBj:2w4x
PDBsum2w4x
PubMed19217614
UniProtQ89ZI2|OGA_BACTN O-GlcNAcase BT_4395 (Gene Name=BT_4395)

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