Homo sapiens
| Assembly | 物理组成 | 蛋白状态 | 分子拷贝数 | 共同组分 | 数据核对 |
|---|---|---|---|---|---|
| 1 | 蛋白单体 | 单体 | 蛋白 1 | 6-{[(2,5-dichlorophenyl)amino]methyl}pyrido[2,3-d]pyrimidine-2,4-diamine × 1 NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE × 1 SULFATE ION × 1 water × 1 | 与蛋白数一致 |
| UniProt名称 | DYR_HUMAN |
| Isoform | — |
| PDB实体 | 1 |
| 链与序列区间 | 作者链 A； PDB构建体 1–186； UniProt 2–187 |
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 | 3l3r |
| 沉积日期 deposition_date | 2009-12-17 |
| 结构标题 title | Structural, Computational and Kinetic Data for Antifolate Interactions Against Pneumocystis jirovecii, Pneumocystis carinii and Human Dihydrofolate Reductase and Their Active Site Mutants |
| 关键词 keywords | dihydrofolate reductase, antifolate, active site mutants, NADP, One-carbon metabolism, Oxidoreductase; OXIDOREDUCTASE |
| 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） | 17.33 Å |
| Rg（电子密度） | 16.04 Å |
| 总 Rg | 17.14 Å |
| 原子数 | 1577 |
| 残基数 | 186 |
| 排除体积 | 28072 ų |
| 最大 q | 0.500 Å⁻¹ |
| 结构域编号 domain_id | d3l3ra_ |
| 类 Class class | c — Alpha and beta proteins (a/b) |
| 折叠类型 Fold fold | c.71 — Dihydrofolate reductase-like |
| 超家族 Superfamily superfamily | c.71.1 — Dihydrofolate reductase-like |
| 家族 Family family | c.71.1.1 — Dihydrofolate reductases |
| 结构域编号 domain_id | 3l3rA00 |
| 类 Class class | 3 — Alpha Beta |
| 架构 Architecture architecture | 40 — 3-Layer(aba) Sandwich |
| 拓扑 Topology topology | 430 — Dihydrofolate Reductase, subunit A |
| 同源超家族 H-superfamily homologous superfamily | 10 — Dihydrofolate Reductase, subunit A |