4JN6
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CRYSTAL STRUCTURE OF THE ALDOLASE-DEHYDROGENASE COMPLEX FROM MYCOBACTERIUM TUBERCULOSIS HRV37
Descriptor:4-hydroxy-2-oxovalerate aldolase (E.C.4.1.3.39), Acetaldehyde dehydrogenase (E.C.1.2.1.10)
Authors:Carere, J., McKenna, S.E., Kimber, M.S., Seah, S.Y.K.
Deposit date:2013-03-14
Release date:2013-05-08
Modification date:2013-12-25
Method:X-RAY DIFFRACTION (1.93 Å)
Cite:Characterization of an Aldolase-Dehydrogenase Complex from the Cholesterol Degradation Pathway of Mycobacterium tuberculosis.
Biochemistry, 52, 2013
4LRS
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CRYSTAL AND SOLUTION STRUCTURES OF THE BIFUNCTIONAL ENZYME (ALDOLASE/ALDEHYDE DEHYDROGENASE) FROM THERMOMONOSPORA CURVATA, REVEAL A COFACTOR-BINDING DOMAIN MOTION DURING NAD+ AND COA ACCOMMODATION WHITHIN THE SHARED COFACTOR-BINDING SITE
Descriptor:4-hydroxy-2-oxovalerate aldolase (E.C.4.1.3.39), Acetaldehyde dehydrogenase (E.C.1.2.1.10), Symmetric aldolase, Cterminal desordered residues
Authors:Fischer, B., Branlant, G., Talfournier, F., Gruez, A.
Deposit date:2013-07-20
Release date:2013-09-04
Method:X-RAY DIFFRACTION (1.55 Å)
Cite:Crystal and solution structures of the bifunctional enzyme (Aldolase/Aldehyde dehydrogenase) from Thermomonospora curvata, reveal a cofactor-binding domain motion during NAD+ and CoA accommodation whithin the shared cofactor-binding site
To be Published
4LRT
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CRYSTAL AND SOLUTION STRUCTURES OF THE BIFUNCTIONAL ENZYME (ALDOLASE/ALDEHYDE DEHYDROGENASE) FROM THERMOMONOSPORA CURVATA, REVEAL A COFACTOR-BINDING DOMAIN MOTION DURING NAD+ AND COA ACCOMMODATION WHITHIN THE SHARED COFACTOR-BINDING SITE
Descriptor:4-hydroxy-2-oxovalerate aldolase (E.C.4.1.3.39), Acetaldehyde dehydrogenase (E.C.1.2.1.10)
Authors:Fischer, B., Branlant, G., Talfournier, F., Gruez, A.
Deposit date:2013-07-20
Release date:2013-09-04
Method:X-RAY DIFFRACTION (1.5 Å)
Cite:Crystal and solution structures of the bifunctional enzyme (Aldolase/Aldehyde dehydrogenase) from Thermomonospora curvata, reveal a cofactor-binding domain motion during NAD+ and CoA accommodation whithin the shared cofactor-binding site
To be Published
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