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PDBsum entry 3f0d
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155 a.a.
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144 a.a.
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145 a.a.
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* Residue conservation analysis
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PDB id:
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Lyase
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Title:
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High resolution crystal structure of 2c-methyl-d-erythritol 2,4- cyclodiphosphatase synthase from burkholderia pseudomallei
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Structure:
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2-c-methyl-d-erythritol 2,4-cyclodiphosphate synthase. Chain: a, b, c, d, e, f. Synonym: mecps, mecdp-synthase. Engineered: yes
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Source:
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Burkholderia pseudomallei. Pseudomonas pseudomallei. Organism_taxid: 28450. Strain: 1710b. Gene: ispf, mecs, bpsl2098. Expressed in: escherichia coli. Expression_system_taxid: 562.
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Resolution:
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1.20Å
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R-factor:
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0.186
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R-free:
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0.209
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Authors:
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Seattle Structural Genomics Center For Infectious Disease (Ssgcid)
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Key ref:
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D.W.Begley
et al.
(2011).
Leveraging structure determination with fragment screening for infectious disease drug targets: MECP synthase from Burkholderia pseudomallei.
J Struct Funct Genomics,
12,
63-76.
PubMed id:
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Date:
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24-Oct-08
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Release date:
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04-Nov-08
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PROCHECK
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Headers
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References
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Q3JRA0
(ISPF_BURP1) -
2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase from Burkholderia pseudomallei (strain 1710b)
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Seq: Struc:
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162 a.a.
155 a.a.
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Enzyme class:
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Chains A, B, C, D, E, F:
E.C.4.6.1.12
- 2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase.
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Reaction:
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4-CDP-2-C-methyl-D-erythritol 2-phosphate = 2-C-methyl-D-erythritol 2,4- cyclic diphosphate + CMP
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4-CDP-2-C-methyl-D-erythritol 2-phosphate
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=
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2-C-methyl-D-erythritol 2,4- cyclic diphosphate
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+
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CMP
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Cofactor:
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Mn(2+) or Mg(2+)
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Molecule diagrams generated from .mol files obtained from the
KEGG ftp site
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J Struct Funct Genomics
12:63-76
(2011)
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PubMed id:
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Leveraging structure determination with fragment screening for infectious disease drug targets: MECP synthase from Burkholderia pseudomallei.
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D.W.Begley,
R.C.Hartley,
D.R.Davies,
T.E.Edwards,
J.T.Leonard,
J.Abendroth,
C.A.Burris,
J.Bhandari,
P.J.Myler,
B.L.Staker,
L.J.Stewart.
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ABSTRACT
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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J.A.Bell,
K.L.Ho,
and
R.Farid
(2012).
Significant reduction in errors associated with nonbonded contacts in protein crystal structures: automated all-atom refinement with PrimeX.
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Acta Crystallogr D Biol Crystallogr,
68,
935-952.
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
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}
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