3so3

Structures of Fab-Protease Complexes Reveal a Highly Specific Non-Canonical Mechanism of Inhibition.

Method: X-RAY DIFFRACTION
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1. 蛋白身份与相关结构 Protein Identity & Related Structures

Suppressor of tumorigenicity 14 protein

Homo sapiens

UniProt Q9Y5Y6

当前结构中的状态

Assembly 物理组成 蛋白状态 分子拷贝数 共同组分 数据核对
1 其他组合 异源复合物 蛋白 3 其他聚合物 1 A11 FAB light chain × 1 A11 FAB heavy chain × 1 beta-D-fructofuranose-(2-1)-alpha-D-glucopyranose × 1 GLYCEROL × 1 water × 3 与蛋白数一致

数据库中的同蛋白其他状态

查看构建体与数据证据
UniProt名称 ST14_HUMAN
Isoform —
PDB实体 1
链与序列区间 作者链 A; PDB构建体 1–241; UniProt 615–855

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。

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2. 结构基本信息 2. Structure Basics

条目编号 entry_id3so3
沉积日期 deposition_date2011-06-29
结构标题 titleStructures of Fab-Protease Complexes Reveal a Highly Specific Non-Canonical Mechanism of Inhibition.
关键词 keywords;antibody-protein, protein-protein, protease inhibitor, disease mutation, glycoprotein, hydrolase, membrane, serine protease, signal-anchor, transmembrane ;; HYDROLASE
实验方法 methodX-RAY DIFFRACTION
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3. Official assembly/model 理论 SAXS Official SAXS Profiles

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。

3so3__assembly_1__model_1

Assembly 1 · Model 1 · CRYSOL 4.1.3-1-20251215 (887e7ef)

下载该曲线 .dat

3so3__assembly_1__model_1 | I(q)

10-2 10-1 106 107 q (1/Angstrom) I(q)
100 个绘图点;横轴和纵轴均采用对数尺度。

3so3__assembly_1__model_1 | P(r) · Pending

新版 assembly/model P(r) 尚未计算 此处仅保留位置,不展示旧数据 r (Angstrom) P(r)
P(r) 将按相同 assembly/model 分别计算和展示。
Rg(Guinier)32.24 Å
Rg(电子密度)32.40 Å
总 Rg32.77 Å
原子数5135
残基数676
排除体积90650 ų
最大 q0.500 Å⁻¹
Assembly Model 结构单元 聚集说明 状态 CRYSOL 操作
1 1 3so3__assembly_1__model_1 trimeric (3) 成功 4.1.3-1-20251215 (887e7ef) 查看 下载
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4. 晶体学与实验 4. Crystallography & Experiment

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5. 实体与聚合物信息 Entities & Polymers (6)

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6. 折叠分类 (SCOP + CATH) 10 domains

SCOP 2.08 (4 domains)

结构域编号 domain_idd3so3a_
类 Class classb — All beta proteins
折叠类型 Fold foldb.47 — Trypsin-like serine proteases
超家族 Superfamily superfamilyb.47.1 — Trypsin-like serine proteases
家族 Family familyb.47.1.2 — Eukaryotic proteases
结构域编号 domain_idd3so3b1
类 Class classb — All beta proteins
折叠类型 Fold foldb.1 — Immunoglobulin-like beta-sandwich
超家族 Superfamily superfamilyb.1.1 — Immunoglobulin
家族 Family familyb.1.1.1 — V set domains (antibody variable domain-like)
结构域编号 domain_idd3so3b2
类 Class classb — All beta proteins
折叠类型 Fold foldb.1 — Immunoglobulin-like beta-sandwich
超家族 Superfamily superfamilyb.1.1 — Immunoglobulin
家族 Family familyb.1.1.2 — C1 set domains (antibody constant domain-like)
结构域编号 domain_idd3so3c_
类 Class classb — All beta proteins
折叠类型 Fold foldb.1 — Immunoglobulin-like beta-sandwich
超家族 Superfamily superfamilyb.1.1 — Immunoglobulin
家族 Family familyb.1.1.1 — V set domains (antibody variable domain-like)

CATH v4.4 (6 domains)

结构域编号 domain_id3so3A01
类 Class class2 — Mainly Beta
架构 Architecture architecture40 — Beta Barrel
拓扑 Topology topology10 — Thrombin, subunit H
同源超家族 H-superfamily homologous superfamily10 — Trypsin-like serine proteases
结构域编号 domain_id3so3A02
类 Class class2 — Mainly Beta
架构 Architecture architecture40 — Beta Barrel
拓扑 Topology topology10 — Thrombin, subunit H
同源超家族 H-superfamily homologous superfamily10 — Trypsin-like serine proteases
结构域编号 domain_id3so3B01
类 Class class2 — Mainly Beta
架构 Architecture architecture60 — Sandwich
拓扑 Topology topology40 — Immunoglobulin-like
同源超家族 H-superfamily homologous superfamily10 — Immunoglobulins
结构域编号 domain_id3so3B02
类 Class class2 — Mainly Beta
架构 Architecture architecture60 — Sandwich
拓扑 Topology topology40 — Immunoglobulin-like
同源超家族 H-superfamily homologous superfamily10 — Immunoglobulins
结构域编号 domain_id3so3C01
类 Class class2 — Mainly Beta
架构 Architecture architecture60 — Sandwich
拓扑 Topology topology40 — Immunoglobulin-like
同源超家族 H-superfamily homologous superfamily10 — Immunoglobulins
结构域编号 domain_id3so3C02
类 Class class2 — Mainly Beta
架构 Architecture architecture60 — Sandwich
拓扑 Topology topology40 — Immunoglobulin-like
同源超家族 H-superfamily homologous superfamily10 — Immunoglobulins
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7. 引用文献 (1)