The crystal structures of pyruvate decarboxylase from Kluyveromyces lactis in the absence of ligands and in the presence of the substrate surrogate pyruvamide
Kutter, S., Konig, S.To be published.
Experimental Data Snapshot
Starting Model: experimental
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Entity ID: 1 | |||||
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Molecule | Chains | Sequence Length | Organism | Details | Image |
Pyruvate decarboxylase | A, B, C [auth D], D [auth E] | 563 | Kluyveromyces lactis NRRL Y-1140 | Mutation(s): 0  EC: 4.1.1.1 | |
UniProt | |||||
Find proteins for Q12629 (Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37)) Explore Q12629  Go to UniProtKB:  Q12629 | |||||
Entity Groups   | |||||
Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
UniProt Group | Q12629 | ||||
Sequence AnnotationsExpand | |||||
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Ligands 2 Unique | |||||
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ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
TPP Query on TPP | E [auth A], G [auth B], I [auth D], K [auth E] | THIAMINE DIPHOSPHATE C12 H19 N4 O7 P2 S AYEKOFBPNLCAJY-UHFFFAOYSA-O | |||
MG Query on MG | F [auth A], H [auth B], J [auth D], L [auth E] | MAGNESIUM ION Mg JLVVSXFLKOJNIY-UHFFFAOYSA-N |
Length ( ? ) | Angle ( ? ) |
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a = 78.36 | ¦Á = 80.1 |
b = 78.48 | ¦Â = 67.72 |
c = 100.57 | ¦Ă = 77.4 |
Software Name | Purpose |
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REFMAC | refinement |
xia2 | data reduction |
XDS | data reduction |
Aimless | data scaling |
MOLREP | phasing |