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Contents |
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* Residue conservation analysis
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PDB id:
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Hydrolase
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Title:
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L-asparaginase from erwinia carotovora in complex with glutamic acid
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Structure:
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L-asparaginase. Chain: a, b, e, f, c, d, g, h, i, j, k, l. Engineered: yes
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Source:
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Pectobacterium atrosepticum. Organism_taxid: 29471. Gene: lans. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
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Resolution:
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2.20Å
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R-factor:
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0.222
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R-free:
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0.267
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Authors:
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O.V.Kravchenko,Y.A.Kislitsin,A.N.Popov,S.V.Nikonov, I.P.Kuranova
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Key ref:
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O.V.Kravchenko
et al.
Crystallographic analysis of l-Asparaginase structures from erwinia carotovora in complex with aspartic and glutamic acids.
To be published,
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Date:
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08-Jul-06
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Release date:
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17-Jul-07
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PROCHECK
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Headers
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References
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Q7WWK9
(Q7WWK9_ERWCT) -
L-asparaginase
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Seq:
Struc:
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349 a.a.
308 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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Enzyme class:
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E.C.3.5.1.1
- Asparaginase.
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Reaction:
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L-asparagine + H2O = L-aspartate + NH3
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L-asparagine
Bound ligand (Het Group name = )
matches with 58.00% similarity
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+
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H(2)O
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=
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L-aspartate
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+
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NH(3)
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Molecule diagrams generated from .mol files obtained from the
KEGG ftp site
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Gene Ontology (GO) functional annotation
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Biological process
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cellular amino acid metabolic process
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2 terms
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Biochemical function
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hydrolase activity
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2 terms
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Links
