Structure of PDB 2xm1 Chain B

Receptor sequence
>2xm1B (length=643) Species: 226186 (Bacteroides thetaiotaomicron VPI-5482) [Search protein sequence]
LQPPPQQLIVQNKTIDLPAVYQLNGGEEANPHAVKVLKELLSGKQSSKKG
MLISIGEKGDKSVRKYSRQIPDHKEGYYLSVNEKEIVLAGNDERGTYYAL
QTFAQLLKDGKLPEVEIKDYPSVRYRGVVEGFYGTPWSHQARLSQLKFYG
KNKMNTYIYGPKDDPYHSAPNWRLPYPDKEAAQLQELVAVANENEVDFVW
AIHPGQDIKWNKEDRDLLLAKFEKMYQLGVRSFAVFFDDISGEGTNPQKQ
AELLNYIDEKFAQVKPDINQLVMCPTEYNKSWSNPNGNYLTTLGDKLNPS
IQIMWTGDRVISDITRDGISWINERIKRPAYIWWNFPVSDYVRDHLLLGP
VYGNDTTIAKEMSGFVTNPMEHAESSKIAIYSVASYAWNPAKYDTWQTWK
DAIRTILPSAAEELECFAMHNSDLGPNGHGYRREESMDIQPAAERFLKAF
KEGKNYDKADFETLQYTFERMKESADILLMNTENKPLIVEITPWVHQFKL
TAEMGEEVLKMVERNESYFLRKYNHVKALQQQMFYIDQTSNQNPYQPGVK
TATRVIKPLIDRTFATVVKFFNQKFNAHLDATTDYMPHKMNLPLQVKANR
VLISPVEIELDAIYPGENIQILSAGLQKAPVKFVRFFVLTIEK
3D structure
PDB2xm1 Inhibition of a Bacterial O-Glcnacase Homologue by Lactone and Lactam Derivatives: Structural, Kinetic and Thermodynamic Analyses.
ChainB
Resolution2.0 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 3.2.1.169: protein O-GlcNAcase.
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 LTM B G135 K166 D242 Y282 V314 W337 N339 D344 G131 K162 D238 Y278 V310 W333 N335 D340 MOAD: Kd=8.5uM
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

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Molecular Function
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Biological Process
External links
PDB RCSB:2xm1, PDBe:2xm1, PDBj:2xm1
PDBsum2xm1
PubMed20689974
UniProtQ89ZI2|OGA_BACTN O-GlcNAcase BT_4395 (Gene Name=BT_4395)

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