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PDBe Entry: 2v9l 
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: 1.23 Å, R-factor: 9.06%, Free R-factor: 12.21%, Spacegroup: P 4 21 2
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15/01/2008, deposition: 24/08/2007, 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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ENTROPY INDEX, METAL-BINDING, OLIGOMERIZATION, ZINC, LYASE, ALDOLASE, CLASS II, CYTOPLASM, CLEAVAGE OF L-RHAMNULOSE-1-PHOSPHATE TO DIHYDROXYACETONEPH BACTERIAL L-RHAMNOSE METABOLISM, INTERFACE DESIGN, SURFACE MUTATION, 2-KETOSE DEGRADATION, PROTEIN-PROTEIN INTERFACE, RARE SUGAR, AGGREGATION, ZINC ENZYME, FIBRILLATION, RHAMNOSE METABOLISM, PROTEIN ENGINEERING
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4.1.2.19 ExPASy BRENDA (A)
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Escherichia coli 562(A)
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Rhamnulose-1-phosphate aldolase (EC 4.1.2.19) P32169 (A)
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A
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1gt7, 1ojr, 2uyu, 2v2b, 2uyv, 2v29, 2v2a, 2v9e, 2v9f, 2v9g, 2v9i, 2v9m, 2v9n, 2v9o
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| A |
RHAMNULOSE-1-PHOSPHATE ALDOLASE |
Protein |
P32169 (RHAD_ECOLI)
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274 |
100% |
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| A |
ZINC ION |
ZN
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| A |
PHOSPHATE ION |
PO4
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| A |
ACETATE ION |
ACT
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| A |
S-1,2-PROPANEDIOL |
PGO
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