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Atomistry » Magnesium » PDB 1k9w-1kk3 » 1kc3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Magnesium » PDB 1k9w-1kk3 » 1kc3 » |
Magnesium in PDB 1kc3: Crystal Structure of Dtdp-6-Deoxy-L-Lyxo-4-Hexulose Reductase (Rmld) in Complex with Nadph and Dtdp-L-RhamnoseEnzymatic activity of Crystal Structure of Dtdp-6-Deoxy-L-Lyxo-4-Hexulose Reductase (Rmld) in Complex with Nadph and Dtdp-L-Rhamnose
All present enzymatic activity of Crystal Structure of Dtdp-6-Deoxy-L-Lyxo-4-Hexulose Reductase (Rmld) in Complex with Nadph and Dtdp-L-Rhamnose:
1.1.1.133; Protein crystallography data
The structure of Crystal Structure of Dtdp-6-Deoxy-L-Lyxo-4-Hexulose Reductase (Rmld) in Complex with Nadph and Dtdp-L-Rhamnose, PDB code: 1kc3
was solved by
W.Blankenfeldt,
I.D.Kerr,
M.F.Giraud,
H.J.Mcmiken,
G.A.Leonard,
C.Whitfield,
P.Messner,
M.Graninger,
J.H.Naismith,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Magnesium Binding Sites:
The binding sites of Magnesium atom in the Crystal Structure of Dtdp-6-Deoxy-L-Lyxo-4-Hexulose Reductase (Rmld) in Complex with Nadph and Dtdp-L-Rhamnose
(pdb code 1kc3). This binding sites where shown within
5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the Crystal Structure of Dtdp-6-Deoxy-L-Lyxo-4-Hexulose Reductase (Rmld) in Complex with Nadph and Dtdp-L-Rhamnose, PDB code: 1kc3: Magnesium binding site 1 out of 1 in 1kc3Go back to Magnesium Binding Sites List in 1kc3
Magnesium binding site 1 out
of 1 in the Crystal Structure of Dtdp-6-Deoxy-L-Lyxo-4-Hexulose Reductase (Rmld) in Complex with Nadph and Dtdp-L-Rhamnose
Mono view Stereo pair view
Reference:
W.Blankenfeldt,
I.D.Kerr,
M.F.Giraud,
H.J.Mcmiken,
G.Leonard,
C.Whitfield,
P.Messner,
M.Graninger,
J.H.Naismith.
Variation on A Theme of Sdr. Dtdp-6-Deoxy-L- Lyxo-4-Hexulose Reductase (Rmld) Shows A New MG2+-Dependent Dimerization Mode. Structure V. 10 773 2002.
Page generated: Tue Aug 13 07:40:57 2024
ISSN: ISSN 0969-2126 PubMed: 12057193 DOI: 10.1016/S0969-2126(02)00770-0 |
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