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 pep-tide, transmembrane topological structure, subcellular localization, protein secondary structure and tertia-ry structure, the enzyme active center structure, and the composition of homologous protein and phyloge-netic relationship of human being and other 6 species.The results show that the CYP2 E1 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 C6778 H10986 N2074 O2429 S374;.It is also found that CYP2E1 is a transmem-brane protein with hydrophobicity and relatively unstable.There are 6 βfold, 6 α-helix, 6 transmem-brane regions and 32 angles in its secondary structure, and It's active center was composed of Asn202 resi-dues, Ser298 residues, Phe205 residues and iron porphyrin ring.The distance of its heme and substrate cat-alytic sites is 0.3-0.6 nm .%采用生物信息学方法对人CYP2E1基因编码蛋白质的结构、理化性质、亲疏水性、信号肽、跨膜结构域、亚细胞定位、二级结构、三级结构、酶活性中心等进行预测，并对人和其他6物种的CYP2E1编码蛋白序列进行系统进化分析．研究结果表明，人CYP2E1编码493个氨基酸组成多肽，其相对分子质量约为172386.6，等电点理论值为7.04，分子式为C6778 H10986 N2074 O2429 S374．该蛋白定位于细胞膜外，属跨膜蛋白，为疏水性不稳定蛋白；该蛋白二级结构有6个β折叠、6个α-螺旋、6个跨膜结构区和32个转角，该酶活性中心由Asn202残基、Ser298残基及Phe205残基与铁卟啉环构成，CYP2E1蛋白血红素铁和底物催化位点之间的距离在0.3～0.6 nm之间．
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