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PDBe Entry: 1fdz view

N-ACETYLNEURAMINATE LYASE IN COMPLEX WITH PYRUVATE VIA BOROHYDRIDE REDUCTION
Summary
Header LYASEsearch
Method X-RAY DIFFRACTION
Experiment Resolution: 2.6 Å, R-factor: 20.0%, Spacegroup: P 32 2 1
Released 22/10/1997, deposition: 08/07/1996, last revision: 24/02/2009
Authors Lawrence, M.C.search; Barbosa, J.A.R.G.search; Smith, B.J.search; Hall, N.E.search; Pilling, P.A.search; Ooi, H.C.search; Marcuccio, S.M.search
Primary citation Structure and mechanism of a sub-family of enzymes related to N-acetylneuraminate lyase.
J.MOL.BIOL.search vol:266, pag:381-399 (1997) [PubMed ID 9047371 ]search
Keywords LYASEsearch, ALDOLASEsearch, OXO-ACID LYASEsearch, ALPHA-KETO-ACID LYASEsearch, CARBON-CARBON LYASEsearch
EC 4.1.3.3 ExPASy BRENDA search (A B C D)
Organism Escherichia coli 562search(A B C D)
UniProt N-acetylneuraminate lyase (EC 4.1.3.3) (N-acetylneuraminic acid aldolase) (N-acetylneuraminate pyruvate-lyase) (Sialic acid lyase) (Sialate lyase) (Sialic acid aldolase) (NALase) P0A6L4search (A B C D)
Solvent A, B, C, D
Polymers
Id Name Type UniProt Residues Observed
A, B, C, D N-ACETYLNEURAMINATE LYASE Protein P0A6L4 (NANA_ECOLI)search
297 98%
Heterogens
Id Name Ligands
A, B, C, D PYRUVIC ACID PYR search
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