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PDB: 3 results

3A4W
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BU of 3a4w by Molmil
Crystal structures of catalytic site mutants of active domain 2 of thermostable chitinase from Pyrococcus furiosus complexed with chito-oligosaccharides
Descriptor: 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, Chitinase, MAGNESIUM ION, ...
Authors:Tsuji, H, Nishimura, S, Inui, T, Ishikawa, K, Nakamura, T, Uegaki, K.
Deposit date:2009-07-22
Release date:2010-06-09
Last modified:2023-11-01
Method:X-RAY DIFFRACTION (1.8 Å)
Cite:Kinetic and crystallographic analyses of the catalytic domain of chitinase from Pyrococcus furiosus- the role of conserved residues in the active site
Febs J., 277, 2010
3AFB
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BU of 3afb by Molmil
Crystal structures of catalytic site mutants of active domain 2 of chitinase from Pyrococcus furiosus
Descriptor: GLYCEROL, MAGNESIUM ION, Putative chitinase, ...
Authors:Tsuji, H.
Deposit date:2010-02-25
Release date:2010-06-09
Last modified:2024-03-13
Method:X-RAY DIFFRACTION (1.76 Å)
Cite:Kinetic and crystallographic analyses of the catalytic domain of chitinase from Pyrococcus furiosus- the role of conserved residues in the active site
Febs J., 277, 2010
3A4X
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BU of 3a4x by Molmil
Crystal structures of catalytic site mutants of active domain 2 of thermostable chitinase from Pyrococcus furiosus complexed with chito-oligosaccharides
Descriptor: 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-alpha-D-glucopyranose, Chitinase, GLYCEROL, ...
Authors:Tsuji, H, Nishimura, S, Inui, T, Ishikawa, K, Nakamura, T, Uegaki, K.
Deposit date:2009-07-22
Release date:2010-06-09
Last modified:2023-11-01
Method:X-RAY DIFFRACTION (1.76 Å)
Cite:Kinetic and crystallographic analyses of the catalytic domain of chitinase from Pyrococcus furiosus- the role of conserved residues in the active site
Febs J., 277, 2010

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