物种未注明
| Assembly | 物理组成 | 蛋白状态 | 分子拷贝数 | 共同组分 | 数据核对 |
|---|---|---|---|---|---|
| 1 | 蛋白同源多聚体 | 同源多聚体 | 蛋白 2 | GLYCEROL × 2 16-hydroxyhexadecanoic acid × 2 water × 2 | 与蛋白数一致 |
| UniProt名称 | LIP_THELA |
| Isoform | — |
| PDB实体 | 1 |
| 链与序列区间 | 作者链 A； PDB构建体 1–269； UniProt 23–291 作者链 B； PDB构建体 1–269； UniProt 23–291 |
页面优先展示蛋白身份、当前 assembly、共同组分、聚集状态和跨 PDB 结构链接。 链映射与序列区间收在“数据证据”中；数据库内部编号、导入时间和 assembly 操作表达式仅用于维护，因此不在读者页面展示。
| 条目编号 entry_id | 4gi1 |
| 沉积日期 deposition_date | 2012-08-08 |
| 结构标题 title | Structure of the complex of three phase partition treated lipase from Thermomyces lanuginosa with 16-hydroxypalmitic acid at 2.4 A resolution |
| 关键词 keywords | Hydrolase, 16-hydroxypalmitic acid; HYDROLASE |
| 实验方法 method | X-RAY DIFFRACTION |
页面只读取最新 assembly 计算结果。每一条曲线都对应明确的 PDB、official biological assembly 和 coordinate model。
Assembly 1 · Model 1 · CRYSOL 4.1.3-1-20251215 (887e7ef)
| Rg（Guinier） | 27.05 Å |
| Rg（电子密度） | 26.11 Å |
| 总 Rg | 26.83 Å |
| 原子数 | 4192 |
| 残基数 | 538 |
| 排除体积 | 73743 ų |
| 最大 q | 0.500 Å⁻¹ |
| 结构域编号 domain_id | d4gi1a_ |
| 类 Class class | c — Alpha and beta proteins (a/b) |
| 折叠类型 Fold fold | c.69 — alpha/beta-Hydrolases |
| 超家族 Superfamily superfamily | c.69.1 — alpha/beta-Hydrolases |
| 家族 Family family | c.69.1.17 — Fungal lipases |
| 结构域编号 domain_id | d4gi1b_ |
| 类 Class class | c — Alpha and beta proteins (a/b) |
| 折叠类型 Fold fold | c.69 — alpha/beta-Hydrolases |
| 超家族 Superfamily superfamily | c.69.1 — alpha/beta-Hydrolases |
| 家族 Family family | c.69.1.17 — Fungal lipases |
| 结构域编号 domain_id | 4gi1A00 |
| 类 Class class | 3 — Alpha Beta |
| 架构 Architecture architecture | 40 — 3-Layer(aba) Sandwich |
| 拓扑 Topology topology | 50 — Rossmann fold |
| 同源超家族 H-superfamily homologous superfamily | 1820 — Alpha/Beta hydrolase fold, catalytic domain |
| 结构域编号 domain_id | 4gi1B00 |
| 类 Class class | 3 — Alpha Beta |
| 架构 Architecture architecture | 40 — 3-Layer(aba) Sandwich |
| 拓扑 Topology topology | 50 — Rossmann fold |
| 同源超家族 H-superfamily homologous superfamily | 1820 — Alpha/Beta hydrolase fold, catalytic domain |