2IUL
Human tACE g13 mutant
- PDB DOI: https://doi.org/10.2210/pdb2IUL/pdb
- Classification: HYDROLASE
- Organism(s): Homo sapiens
- Expression System: Cricetulus griseus
- Mutation(s): Yes
- Deposited: 2006-06-06 Released: 2006-10-25
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 2.01 Å
- R-Value Free: 0.220
- R-Value Work: 0.180
- R-Value Observed: 0.182
This is version 2.1 of the entry. See complete history.
Macromolecules
Find similar proteins by:
(by identity cutoff) | 3D Structure
Entity ID: 1 | |||||
|---|---|---|---|---|---|
| Molecule | Chains | Sequence Length | Organism | Details | Image |
| ANGIOTENSIN-CONVERTING ENZYME | 591 | Homo sapiens | Mutation(s): 4 EC: 3.4.15.1 (PDB Primary Data), 3.2.1 (PDB Primary Data) |  | |
UniProt & NIH Common Fund Data Resources | |||||
Find proteins for P12821 (Homo sapiens) Explore P12821 Go to UniProtKB: P12821 | |||||
PHAROS: P12821 GTEx: ENSG00000159640 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | P12821 | ||||
Sequence AnnotationsExpand | |||||
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Oligosaccharides
Entity ID: 2 | |||||
|---|---|---|---|---|---|
| Molecule | Chains | Length | 2D Diagram | Glycosylation | 3D Interactions |
| beta-D-mannopyranose-(1-3)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose | B | 5 |  | N-Glycosylation | |
Glycosylation Resources | |||||
GlyTouCan: G51347YJ GlyCosmos: G51347YJ GlyGen: G51347YJ | |||||
Small Molecules
| Ligands 4 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| NAG Query on NAG | C [auth A] | 2-acetamido-2-deoxy-beta-D-glucopyranose C8 H15 N O6 OVRNDRQMDRJTHS-FMDGEEDCSA-N |  | ||
| ZN Query on ZN | H [auth A] | ZINC ION Zn PTFCDOFLOPIGGS-UHFFFAOYSA-N |  | ||
| ACT Query on ACT | D [auth A], E [auth A] | ACETATE ION C2 H3 O2 QTBSBXVTEAMEQO-UHFFFAOYSA-M |  | ||
| CL Query on CL | F [auth A], G [auth A] | CHLORIDE ION Cl VEXZGXHMUGYJMC-UHFFFAOYSA-M |  | ||
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 2.01 Å
- R-Value Free: 0.220
- R-Value Work: 0.180
- R-Value Observed: 0.182
- Space Group: P 21 21 21
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 56.633 | α = 90 |
| b = 84.723 | β = 90 |
| c = 134.466 | γ = 90 |
| Software Name | Purpose |
|---|---|
| REFMAC | refinement |
| HKL-2000 | data reduction |
| HKL-2000 | data scaling |
Entry History
Deposition Data
- Released Date: 2006-10-25 Deposition Author(s): Watermeyer, J.M., Sewell, B.T., Natesh, R., Corradi, H.R., Acharya, K.R., Sturrock, E.D.
Revision History (Full details and data files)
- Version 1.0: 2006-10-25
Type: Initial release - Version 1.1: 2011-05-08
Changes: Version format compliance - Version 1.2: 2011-07-13
Changes: Version format compliance - Version 2.0: 2020-07-29
Type: Remediation
Reason: Carbohydrate remediation
Changes: Advisory, Atomic model, Data collection, Derived calculations, Other, Structure summary - Version 2.1: 2023-12-13
Changes: Advisory, Data collection, Database references, Refinement description, Structure summary
