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*
Residue conservation analysis
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| PDB id: |
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3b7m
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| Name: |
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Hydrolase
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| Title: |
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Crystal structure of a meso-active thermo-stable cellulase (mt cel12a) derived by making non-contiguous mutations in the active surface of the cel12a cellulase of rhodothermus marinus
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Structure: |
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Cellulase. Chain: a, b, c, d. Engineered: yes
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Source:
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Rhodothermus marinus. Organism_taxid: 29549. Gene: cela. Expressed in: escherichia coli. Expression_system_taxid: 562.
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UniProt:
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Chains A,
B,
C,
D:
O33897
(O33897_RHOMR)
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| Seq: |
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260 a.a. |
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| Struc: |
216 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 50 residue positions (black
crosses)
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Enzyme class:
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Reaction:
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Endohydrolysis of 1,4-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.
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Resolution:
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2.10Å
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R-factor:
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0.189
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R-free:
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0.238
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Authors:
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S.Karthikeyan,P.Guptasarma
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Key ref:
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d.kapoor
et al.
Transplantation of the active surface of a mesophile cellulase onto the structural scaffold of a homologous thermophile cellulase through engineering of a surface beta sheet.
To be Published,
xsi:nil="true" />.
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Date:
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31-Oct-07
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Release date:
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27-Nov-07
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Related entries:
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crystal structure of rhodothermus marinus cel12a
crystal structure of trichoderma reesei cel12a
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Quick_links |
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Procheck |
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Surface |
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216 a.a.
