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PDBe Entry: 2uyv 
L-RHAMNULOSE-1-PHOSPHATE ALDOLASE FROM ESCHERICHIA COLI (MUTANT Q6Y-E192A)
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LYASE
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X-RAY DIFFRACTION
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Resolution: 2.2 Å, R-factor: 20.43%, Free R-factor: 24.42%, Spacegroup: I 2 2 2
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15/01/2008, deposition: 20/04/2007, last revision: 24/02/2009
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Grueninger, D.; Schulz, G.E.
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Designed Protein-Protein Association.
SCIENCE vol:319, pag:206 (2008) [PubMed ID 18187656 ]
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AGGREGATION, ZINC ENZYME, FIBRILLATION, METAL-BINDING, OLIGOMERIZATION, INTERFACE DESIGN, SURFACE MUTATION, 2-KETOSE DEGRADATION, PROTEIN-PROTEIN INTERFACE, ZINC, LYASE, ALDOLASE, CLASS II, RARE SUGAR, CLEAVAGE OF L-RHAMNULOSE-1-PHOSPHATE TO DIHYDROXYACETONEPH BACTERIAL L-RHAMNOSE METABOLISM, RHAMNOSE METABOLISM, PROTEIN ENGINEERING
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4.1.2.19 ExPASy BRENDA (A B C D)
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Escherichia coli 562(A B C D)
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Rhamnulose-1-phosphate aldolase (EC 4.1.2.19) P32169 (A B C D)
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A, B, C, D
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1gt7, 1ojr, 2uyu
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| A, B, C, D |
RHAMNULOSE-1-PHOSPHATE ALDOLASE |
Protein |
P32169 (RHAD_ECOLI)
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274 |
100% |
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| A, B, C, D |
L(+)-TARTARIC ACID |
TLA
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| A, B, C, D |
ZINC ION |
ZN
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