2ae4
Glutaryl 7-Aminocephalosporanic Acid Acylase: mutational study of activation mechanism
1. Protein Identity and Related Structures Protein Identity & Related Structures
No usable UniProt protein identity is available for this entry.
The relationship tables retain this entry's assembly and composition data, but cross-PDB links for the same protein cannot be established reliably without a unified protein identity.
Assembly Composition of the Current Entry
| Assembly | Physical composition | Protein state | 蛋白 / DNA / RNA / 其他Polymer | Data consistency |
|---|---|---|---|---|
| 1 | Protein heterocomplex | Heteromer | 2 / 0 / 0 / 0 | Consistent with protein count |
The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.
2. Structure Basics 2. Structure Basics
| Entry ID entry_id | 2ae4 |
| Deposition date deposition_date | 2005-07-21 |
| Structure title title | Glutaryl 7-Aminocephalosporanic Acid Acylase: mutational study of activation mechanism |
| Keywords keywords | autoproteolysis, precursor activation, intermediate structure, cephalosporin acylase, HYDROLASE; HYDROLASE |
| Experimental Method method | X-RAY DIFFRACTION |
3. Official assembly/model SAXS Official SAXS Profiles
This page reads only the latest assembly calculations. Every curve maps to an explicit PDB entry, official biological assembly and coordinate model.
2ae4__assembly_1__model_1
Assembly 1 · Model 1 · CRYSOL 4.1.3-1-20251215 (887e7ef)
2ae4__assembly_1__model_1 | I(q)
2ae4__assembly_1__model_1 | P(r) · Pending
| Rg（Guinier） | 26.76 Å |
| Rg (electron density) | 25.74 Å |
| Total Rg | 26.57 Å |
| Atom count | 5382 |
| Residues | 682 |
| Excluded volume | 94369 ų |
| Maximum q | 0.500 Å⁻¹ |
4. Crystallography and Experiment 4. Crystallography & Experiment
5. Entities and Polymers Entities & Polymers (5)
6. Fold Classification (SCOP + CATH) 4 domains
CATH v4.4 (4 domains)
| Domain ID domain_id | 2ae4A00 |
| Class class | 1 — Mainly Alpha |
| Architecture architecture | 10 — Orthogonal Bundle |
| Topology topology | 439 — Penicillin Amidohydrolase; domain 1 |
| Homologous superfamily homologous superfamily | 10 — Penicillin Amidohydrolase, domain 1 |
| Domain ID domain_id | 2ae4B01 |
| Class class | 3 — Alpha Beta |
| Architecture architecture | 60 — 4-Layer Sandwich |
| Topology topology | 20 — Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1 |
| Homologous superfamily homologous superfamily | 10 — Aminohydrolase, N-terminal nucleophile (Ntn) domain |
| Domain ID domain_id | 2ae4B02 |
| Class class | 2 — Mainly Beta |
| Architecture architecture | 30 — Roll |
| Topology topology | 120 — Penicillin G acylase, beta-roll domain |
| Homologous superfamily homologous superfamily | 10 — Aminohydrolase, N-terminal nucleophile (Ntn) domain, beta-sheet knob region |
| Domain ID domain_id | 2ae4B03 |
| Class class | 1 — Mainly Alpha |
| Architecture architecture | 10 — Orthogonal Bundle |
| Topology topology | 1400 — Penicillin amidase (Acylase) alpha subunit, N-terminal domain |
| Homologous superfamily homologous superfamily | 10 — Aminohydrolase, alpha-helical knob region |