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PDBsum entry 2y4l
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* Residue conservation analysis
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PDB id:
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Transferase
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Title:
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Mannosylglycerate synthase in complex with manganese and gdp
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Structure:
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Mannosylglycerate synthase. Chain: a, b. Fragment: residues 1-382. Synonym: mannosyl-3-phosphoglycerate synthase. Engineered: yes. Mutation: yes. Other_details: c-terminal truncation of last 15 residues
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Source:
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Rhodothermus marinus. Organism_taxid: 518766. Strain: dsm 4252. Expressed in: escherichia coli. Expression_system_taxid: 511693. Expression_system_variant: tuner.
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Resolution:
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2.80Å
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R-factor:
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0.189
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R-free:
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0.220
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Authors:
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M.M.Nielsen,M.D.L.Suits,M.Yang,C.S.Barry,C.Martinez-Fleites, L.E.Tailford,J.E.Flint,B.G.Davis,G.J.Davies,H.J.Gilbert
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Key ref:
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M.M.Nielsen
et al.
(2011).
Substrate and metal ion promiscuity in mannosylglycerate synthase.
J Biol Chem,
286,
15155-15164.
PubMed id:
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Date:
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07-Jan-11
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Release date:
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02-Feb-11
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Supersedes:
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PROCHECK
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Headers
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References
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D0MI02
(D0MI02_RHOM4) -
Mannosylglycerate synthase from Rhodothermus marinus (strain ATCC 43812 / DSM 4252 / R-10)
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Seq: Struc:
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397 a.a.
380 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 2 residue positions (black
crosses)
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Enzyme class:
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E.C.2.4.1.217
- mannosyl-3-phosphoglycerate synthase.
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Reaction:
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(2R)-3-phosphoglycerate + GDP-alpha-D-mannose = 2-O-(alpha-D-mannosyl)-3- phosphoglycerate + GDP + H+
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(2R)-3-phosphoglycerate
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GDP-alpha-D-mannose
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=
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2-O-(alpha-D-mannosyl)-3- phosphoglycerate
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GDP
Bound ligand (Het Group name = )
corresponds exactly
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H(+)
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Cofactor:
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Mg(2+)
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Molecule diagrams generated from .mol files obtained from the
KEGG ftp site
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J Biol Chem
286:15155-15164
(2011)
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PubMed id:
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Substrate and metal ion promiscuity in mannosylglycerate synthase.
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M.M.Nielsen,
M.D.Suits,
M.Yang,
C.S.Barry,
C.Martinez-Fleites,
L.E.Tailford,
J.E.Flint,
C.Dumon,
B.G.Davis,
H.J.Gilbert,
G.J.Davies.
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ABSTRACT
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');
}
}
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