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PDB: 4 results

4OVW
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BU of 4ovw by Molmil
ENDOGLUCANASE I COMPLEXED WITH EPOXYBUTYL CELLOBIOSE
Descriptor: 2-acetamido-2-deoxy-beta-D-glucopyranose, 4-(beta-D-glucopyranosyloxy)-2,2-dihydroxybutyl propanoate, ENDOGLUCANASE I
Authors:Davies, G.J, Schulein, M.
Deposit date:1997-10-06
Release date:1998-04-08
Last modified:2024-04-03
Method:X-RAY DIFFRACTION (2.3 Å)
Cite:Structure of the endoglucanase I from Fusarium oxysporum: native, cellobiose, and 3,4-epoxybutyl beta-D-cellobioside-inhibited forms, at 2.3 A resolution.
Biochemistry, 36, 1997
3OVW
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BU of 3ovw by Molmil
ENDOGLUCANASE I NATIVE STRUCTURE
Descriptor: 2-acetamido-2-deoxy-beta-D-glucopyranose, ENDOGLUCANASE I
Authors:Davies, G.J, Schulein, M.
Deposit date:1997-10-06
Release date:1998-04-08
Last modified:2024-04-03
Method:X-RAY DIFFRACTION (2.3 Å)
Cite:Structure of the endoglucanase I from Fusarium oxysporum: native, cellobiose, and 3,4-epoxybutyl beta-D-cellobioside-inhibited forms, at 2.3 A resolution.
Biochemistry, 36, 1997
2OVW
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BU of 2ovw by Molmil
ENDOGLUCANASE I COMPLEXED WITH CELLOBIOSE
Descriptor: 2-acetamido-2-deoxy-beta-D-glucopyranose, ENDOGLUCANASE I, beta-D-glucopyranose-(1-4)-beta-D-glucopyranose
Authors:Sulzenbacher, G, Davies, G.J, Schulein, M.
Deposit date:1997-04-04
Release date:1998-04-08
Last modified:2024-04-03
Method:X-RAY DIFFRACTION (2.3 Å)
Cite:Structure of the endoglucanase I from Fusarium oxysporum: native, cellobiose, and 3,4-epoxybutyl beta-D-cellobioside-inhibited forms, at 2.3 A resolution.
Biochemistry, 36, 1997
1OVW
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BU of 1ovw by Molmil
ENDOGLUCANASE I COMPLEXED WITH NON-HYDROLYSABLE SUBSTRATE ANALOGUE
Descriptor: 2-acetamido-2-deoxy-beta-D-glucopyranose, 4-thio-beta-D-glucopyranose-(1-4)-4-thio-beta-D-glucopyranose-(1-4)-1,4-dithio-beta-D-glucopyranose, ENDOGLUCANASE I
Authors:Sulzenbacher, G, Davies, G.J, Schulein, M.
Deposit date:1996-10-17
Release date:1997-10-29
Last modified:2024-04-03
Method:X-RAY DIFFRACTION (2.7 Å)
Cite:Structure of the Fusarium oxysporum endoglucanase I with a nonhydrolyzable substrate analogue: substrate distortion gives rise to the preferred axial orientation for the leaving group.
Biochemistry, 35, 1996

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