Abstract: The nucleotide and amino acid sequences of CYP2E1 protein (GenBank accession number: NC000010.11 and NM000773.3) from human being have been analyzed and predicted by bioinformatics in the following aspects: physicochemical properties, hydrophilicity and hydrophobicity, the signal peptide, transmembrane topological structure, subcellular localization, protein secondary structure and tertiary structure, the enzyme active center structure, and the composition of homologous protein and phylogenetic relationship of human being and other 6 species. The results show that the CYP2E1 gene encodes a 493 amino acid polypeptides with the estimated relative molecular weight 172 386.6, the theoretical PI of 7.04 and the structural formula of C₆₇₇₈H₁₀₉₈₆N₂₀₇₄O₂₄₂₉S₃₇₄;. It is also found that CYP2E1 is a transmembrane protein with hydrophobicity and relatively unstable. There are 6 β fold, 6 α-helix, 6 transmembrane regions and 32 angles in its secondary structure, and It's active center was composed of Asn₂₀₂ residues, Ser₂₉₈ residues, Phe₂₀₅ residues and iron porphyrin ring. The distance of its heme and substrate catalytic sites is 0.3-0.6 nm .

Key words: human cytochrome P4502E1；bioinformatics; sequence analysis