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PDBsum entry 4ais
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PDB id:
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Hydrolase
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Title:
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A complex structure of btgh84
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Structure:
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O-glcnacase bt_4395. Chain: a, b. Synonym: btgh84, beta-n-acetylhexosaminidase, beta-hexosaminidase gh84, hexosaminidase b, n-acetyl-beta-glucosaminidase. Engineered: yes
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Source:
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Bacteroides thetaiotaomicron vpi-5482. Organism_taxid: 226186. Atcc: 29148. Expressed in: escherichia coli. Expression_system_taxid: 511693.
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Resolution:
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2.00Å
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R-factor:
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0.196
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R-free:
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0.244
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Authors:
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Y.He,G.J.Davies
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Key ref:
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M.S.Macauley
et al.
(2012).
Metabolism of vertebrate amino sugars with N-glycolyl groups: intracellular β-O-linked N-glycolylglucosamine (GlcNGc), UDP-GlcNGc, and the biochemical and structural rationale for the substrate tolerance of β-O-linked β-N-acetylglucosaminidase.
J Biol Chem,
287,
28882-28897.
PubMed id:
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Date:
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13-Feb-12
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Release date:
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20-Jun-12
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PROCHECK
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Headers
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References
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Q89ZI2
(OGA_BACTN) -
O-GlcNAcase BT_4395 from Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 / VPI-5482 / E50)
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Seq:
Struc:
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737 a.a.
637 a.a.*
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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*
PDB and UniProt seqs differ
at 14 residue positions (black
crosses)
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Enzyme class:
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E.C.3.2.1.169
- protein O-GlcNAcase.
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Reaction:
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1.
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3-O-(N-acetyl-beta-D-glucosaminyl)-L-seryl-[protein] + H2O = N-acetyl-D-glucosamine + L-seryl-[protein]
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2.
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3-O-(N-acetyl-beta-D-glucosaminyl)-L-threonyl-[protein] + H2O = L-threonyl-[protein] + N-acetyl-D-glucosamine
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3-O-(N-acetyl-beta-D-glucosaminyl)-L-seryl-[protein]
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+
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H2O
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=
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N-acetyl-D-glucosamine
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+
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L-seryl-[protein]
Bound ligand (Het Group name = )
matches with 40.00% similarity
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3-O-(N-acetyl-beta-D-glucosaminyl)-L-threonyl-[protein]
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+
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H2O
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=
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L-threonyl-[protein]
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+
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N-acetyl-D-glucosamine
Bound ligand (Het Group name = )
matches with 40.00% similarity
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Molecule diagrams generated from .mol files obtained from the
KEGG ftp site
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J Biol Chem
287:28882-28897
(2012)
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PubMed id:
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Metabolism of vertebrate amino sugars with N-glycolyl groups: intracellular β-O-linked N-glycolylglucosamine (GlcNGc), UDP-GlcNGc, and the biochemical and structural rationale for the substrate tolerance of β-O-linked β-N-acetylglucosaminidase.
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M.S.Macauley,
J.Chan,
W.F.Zandberg,
Y.He,
G.E.Whitworth,
K.A.Stubbs,
S.A.Yuzwa,
A.J.Bennet,
A.Varki,
G.J.Davies,
D.J.Vocadlo.
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ABSTRACT
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Links
